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Database: UniProt
Entry: A0A136N310_9BACT
LinkDB: A0A136N310_9BACT
Original site: A0A136N310_9BACT 
ID   A0A136N310_9BACT        Unreviewed;       426 AA.
AC   A0A136N310;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=UZ09_BCD002000380 {ECO:0000313|EMBL:KXK40535.1};
OS   Bacteroidetes bacterium OLB9.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1617420 {ECO:0000313|EMBL:KXK40535.1, ECO:0000313|Proteomes:UP000070267};
RN   [1] {ECO:0000313|EMBL:KXK40535.1, ECO:0000313|Proteomes:UP000070267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB9 {ECO:0000313|EMBL:KXK40535.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KXK40535.1}.
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DR   EMBL; LNBW01000011; KXK40535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136N310; -.
DR   STRING; 1617420.UZ09_BCD002000380; -.
DR   PATRIC; fig|1617420.3.peg.407; -.
DR   Proteomes; UP000070267; 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   ECO:0000313|EMBL:KXK40535.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          178..418
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   COILED          74..108
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   426 AA;  48202 MW;  A00E94090D2A02E9 CRC64;
     MLEISTIREH KDRVVEGLKK RNVDTTLLEL LDTIVTTDDL RKSTQTTLDN LLSQSNKMAS
     EIGQLFKSGK TQEADTLKGK VTELKDDIKE YENKLRSIKE SLDDMLLQIP NVPHSSVPAG
     KGAEDNEVYK NWGQPFPQLM DGALPHWELA EKYNIISFKD GVKLTGSGFP VYKGKGARLQ
     RALINFFLDE ASKAGFNEIQ PPLMVNKDSA RATGQLPDKE GQMYYVEKDD FYLIPTAEVP
     VTNLYRDVIL QKSDFPIKLT GYTPCFRREA GSYGSDVKGL NRLHQFDKVE IVWMDLPDHS
     YDVLMEMLKH VEGLLEKLEL PYRILRLCGG DTGFNSALTF DFETWSAAQE RWLEVSSVSN
     FETFQANRMH LRFKDEDGKT RLAHTLNGSA LALARIVATL LENHQTPSGI KIPKALVPYT
     GFDFIN
//
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