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Database: UniProt
Entry: A0A0G0MM73_9BACT
LinkDB: A0A0G0MM73_9BACT
Original site: A0A0G0MM73_9BACT 
ID   A0A0G0MM73_9BACT        Unreviewed;       413 AA.
AC   A0A0G0MM73;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=US96_C0025G0008 {ECO:0000313|EMBL:KKQ74799.1};
OS   Candidatus Woesebacteria bacterium GW2011_GWB1_38_5b.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1618569 {ECO:0000313|EMBL:KKQ74799.1, ECO:0000313|Proteomes:UP000034181};
RN   [1] {ECO:0000313|EMBL:KKQ74799.1, ECO:0000313|Proteomes:UP000034181}
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:KKQ74799.1}.
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DR   EMBL; LBUZ01000025; KKQ74799.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0MM73; -.
DR   PATRIC; fig|1618569.3.peg.602; -.
DR   Proteomes; UP000034181; 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:KKQ74799.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          126..395
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   COILED          40..90
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   413 AA;  47053 MW;  503C4DE9EC6AC13A CRC64;
     MFDIKYIREN PERVEKAAKD KGVTLDLDEI LEIDKKTQIL RLAQQKLLEE RNKAAKHKDK
     EKGKKIKEEI EELEKELLPL EKKLKELLLS IPNIAKSDVK SGKDETENEV IKKVGDIPKF
     DFEALDHMDL GESLDIIDVD RASRVSGTRF AYLKNEAVLL EFALVSYALQ ILTKEGFIPV
     VPPTLVNTEV MRGLGYMEAG GSEDMFHIPS DKLTLVGTAE HSIVPMHMGE VLNVKDLPKR
     YVGFSSAFRR EAGSYGKDTR GILRVHQFDK VEMVSFVEEG KDDKEHEYLL SLEEKLFQAL
     EIPYRVVKMC TGDLGFPAAR KYDIEAWMPG QKTYREVTSV STVTSFQSRR LKIRYQDNGE
     RKYVNILNGT AFAIGRTIIA ILENYQNKDR SIAVPDALQK YMFGVKKISL KKG
//
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