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Database: UniProt
Entry: A0A1G2H520_9BACT
LinkDB: A0A1G2H520_9BACT
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ID   A0A1G2H520_9BACT        Unreviewed;       439 AA.
AC   A0A1G2H520;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=A2827_00960 {ECO:0000313|EMBL:OGZ57420.1};
OS   Candidatus Spechtbacteria bacterium RIFCSPHIGHO2_01_FULL_43_30.
OC   Bacteria; Candidatus Spechtbacteria.
OX   NCBI_TaxID=1802158 {ECO:0000313|EMBL:OGZ57420.1, ECO:0000313|Proteomes:UP000177932};
RN   [1] {ECO:0000313|EMBL:OGZ57420.1, ECO:0000313|Proteomes:UP000177932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGZ57420.1}.
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DR   EMBL; MHOD01000031; OGZ57420.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2H520; -.
DR   STRING; 1802158.A2827_00960; -.
DR   Proteomes; UP000177932; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OGZ57420.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          200..423
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   COILED          30..101
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   439 AA;  50210 MW;  FD5CE7A8F96DE4D4 CRC64;
     MIDLKLLREK PEIFKKAARN KNFEIDIDKI LDLDRKRRDA ARAVDNLRAE QNSASEIIAG
     EKDKDEKKDI IGKMRNLKAD LEKSEESLKN IDAELSSLLM QIPNVPFDNV PVGKNDKDNV
     VLREVGKKQI FAFEPKDYMK IAKQRGWIDV ERASKVSGSR FGYIKGELAL LEFAIIRYVF
     DFLMNSERLN KVIQSAACDV RDTAFMPVLP PVVVKPEYMD AMGFLTGDIA EDMYFLEKDN
     LYLVGTSEQS IGPMHSGETF NDSNLPLRYV GFSTCFRREA GSYGKDTKGI LRVHQFDKIE
     MISFCHPEKS RDEHRFLLAL NEAMMNEFEL PYRVVHISTG DMGLSKAEQF DIETWIPSEN
     TYRETHSASN ITDFQARRLN IKHKGNDKSG YVHMLNATAF AIGRILIAII ENFQTEDAKV
     KIPKELQSYL GRVEIPSQK
//
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