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Database: UniProt
Entry: A0A0G0AQS4_9BACT
LinkDB: A0A0G0AQS4_9BACT
Original site: A0A0G0AQS4_9BACT 
ID   A0A0G0AQS4_9BACT        Unreviewed;       413 AA.
AC   A0A0G0AQS4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=UR43_C0003G0097 {ECO:0000313|EMBL:KKP53776.1};
OS   candidate division TM6 bacterium GW2011_GWF2_33_332.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=1619080 {ECO:0000313|EMBL:KKP53776.1, ECO:0000313|Proteomes:UP000034634};
RN   [1] {ECO:0000313|EMBL:KKP53776.1, ECO:0000313|Proteomes:UP000034634}
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:KKP53776.1}.
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DR   EMBL; LBPE01000003; KKP53776.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0AQS4; -.
DR   PATRIC; fig|1619080.3.peg.469; -.
DR   Proteomes; UP000034634; 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:KKP53776.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          165..402
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   COILED          30..97
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   413 AA;  46972 MW;  73E22791CD1F139D CRC64;
     MIDLSLLREN CETIRSLILK KDPKFDISRL IILDEQVREM RSAVENLRKD RNEISKSASG
     GLSEELRNRS IEVGKELKIK EKLLEELEEE FKKLALTCPN ILMEEVQEGG KENNKAVKTF
     SKKPSFDFEP KNHVELNKTL DWFDFDAATK IAGGNFVLYK KEAVKLIYAL TQLMLKNNAK
     HGFEPVIPPY LATTKSLTNS SNLPKFAEDV YSVPADDLYL IPTAEVSLTN IHADSILNVE
     QLPLRYTAWT GCFRREAGGY GSLERGLIRI HQFEKVELYS IVHPQNSAAE LDYMVECAEN
     ILQQLGLHYQ VSLLAAQDCS FASAKTYDIE VWLPGQQKYY EVSSASNCTD FQARRAGIRF
     RESATAKPQL AHTLNTSSLA LPRLMVALME TYQQEDGTIK FPKILQEMMD NLW
//
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