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Database: UniProt
Entry: A0A0G1GT88_9BACT
LinkDB: A0A0G1GT88_9BACT
Original site: A0A0G1GT88_9BACT 
ID   A0A0G1GT88_9BACT        Unreviewed;       421 AA.
AC   A0A0G1GT88;
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=UW27_C0003G0044 {ECO:0000313|EMBL:KKT38296.1};
OS   Parcubacteria group bacterium GW2011_GWA1_44_13.
OC   Bacteria.
OX   NCBI_TaxID=1618788 {ECO:0000313|EMBL:KKT38296.1, ECO:0000313|Proteomes:UP000034180};
RN   [1] {ECO:0000313|EMBL:KKT38296.1, ECO:0000313|Proteomes:UP000034180}
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:KKT38296.1}.
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DR   EMBL; LCHR01000003; KKT38296.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1GT88; -.
DR   PATRIC; fig|1618788.3.peg.252; -.
DR   Proteomes; UP000034180; 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   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKT38296.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          137..407
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   421 AA;  47641 MW;  000650DC47C90DD2 CRC64;
     MLDIKFIREN AELVKEAAQK KNIAFDVQEL LSADDNRKAI LAEVEAMRGK QNEIADSVPR
     AENVEAREKL IAESKSLKDI LQAKELELTA AMHVWQALMV QVPNLPDVSV PEGKEDSDNV
     EVRTWGTIPK FSFTPKDHIE LFEKHDMADF ERGTKVAGFR GYVLKGDGAR LVFALSQFVL
     NELSKENFIP MMVPSLVRRA PLVGTGFLPQ GEEDLYKTQD GDFLAGTAEV GTMGYHMDEV
     LSLSDLPKKY LSFSTSFRRE AGSHSKDTKG LIRVHEFFKW EQVILCEASH EESVKFHEYL
     TENSEKLMQK LGIPYHVVLN CGGDLGLGQV KKYDIEAWVP SQNTYRETHS ASYFHDFQTR
     RLNIRYKDNE GKLRFAHSLN NTAIAMPRIL VPLVENYQNA DGSITIPEVL RPYMGGKEKI
     G
//
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