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Database: UniProt
Entry: A0A0G1HLW5_9BACT
LinkDB: A0A0G1HLW5_9BACT
Original site: A0A0G1HLW5_9BACT 
ID   A0A0G1HLW5_9BACT        Unreviewed;       421 AA.
AC   A0A0G1HLW5;
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};
GN   ORFNames=UV91_C0001G0066 {ECO:0000313|EMBL:KKT11854.1};
OS   Candidatus Nomurabacteria bacterium GW2011_GWF2_43_24.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1618778 {ECO:0000313|EMBL:KKT11854.1, ECO:0000313|Proteomes:UP000033907};
RN   [1] {ECO:0000313|EMBL:KKT11854.1, ECO:0000313|Proteomes:UP000033907}
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:KKT11854.1}.
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DR   EMBL; LCGH01000001; KKT11854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1HLW5; -.
DR   PATRIC; fig|1618778.3.peg.66; -.
DR   Proteomes; UP000033907; 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:KKT11854.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          175..407
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   COILED          37..94
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   421 AA;  48119 MW;  41FC7D9C7030530E CRC64;
     MLDIKFIREN KDVVQSGAKK KHIDVDIDAL IGLDDERLKI LKEVEELRSE VNRVSNDIAR
     DQDPALKIQL IEEMRAVKEE IKGKEEKLKA IMDDWRKFML QVPNVPDISV PEGNSDADNQ
     EVKVWGDKPA FNFEPKDHIE IMTALKMADF ERGTKVHGFR GYFLINDGVL LSFAIWNYAM
     DFFRTKDFSP VIPPVIVRKD SFVGTGYLPQ GEEDLYKTQG GEYLAGTSEV PIMAIHAGEI
     LDKNSFPFKY LGFSPCFRRE AGSHGKDVKG LIRVNEFYKV EQVVLCEASH EISVKFHEEI
     NRNMEEFIES LKIPYHTVIN CGGDLGLGQV KKYDVELWVP KENKYREIGS ASYFHDFQTR
     RFGIRYKDEE GKINYAHSMN ATAIATPRIL VSLIENCQQA DGSVKIPEVL RPYMGGKEVI
     K
//
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