ID A0A0L0LB43_9BACT Unreviewed; 427 AA.
AC A0A0L0LB43;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-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 Name=serS {ECO:0000313|EMBL:KND47258.1};
GN ORFNames=AB199_02420 {ECO:0000313|EMBL:KND47258.1};
OS Parcubacteria bacterium C7867-004.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659198 {ECO:0000313|EMBL:KND47258.1, ECO:0000313|Proteomes:UP000036787};
RN [1] {ECO:0000313|EMBL:KND47258.1, ECO:0000313|Proteomes:UP000036787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-004 {ECO:0000313|EMBL:KND47258.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(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:KND47258.1}.
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DR EMBL; LFCN01000006; KND47258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LB43; -.
DR STRING; 1659198.AB199_02420; -.
DR PATRIC; fig|1659198.3.peg.452; -.
DR Proteomes; UP000036787; 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:KND47258.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 136..411
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT COILED 30..100
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 427 AA; 48809 MW; 3255A6198E959BCE CRC64;
MLDIHFIREN ADLVKAGAAK KHIEIDIDRL LAVDDERKVL RQQLDEKRAE QNRASQTIAL
AKGEEKEKLL EAMRFVKESM QELEEKYKAA LEEWQKLMLL VPNLPDMTVP DGDSDNDNVE
VRVWGDRKEF SFTPKDHVEL MTNNGMADFE RGAKVAGFRG YFLKGDGAIL QFGIMQFLQN
HFVQKNAKGD TWIPMVVPSL VRREGFMGTG YLPQSEDDLY KTQDSEYLAG TGEVATMAFH
LDETLEKGSL PIKYFSFSPC FRREIGAHGK DTKGLVRVHE FYKFEQVVLS EASHEESVRL
HEELTVNAEE ILKVLDIPYH VVVNCGGDLG LGQVKKYDIE AWMPGENKYR ETHSSSYFHD
FQTRRLNIRY RDEDGTLKFA HSLNNTALAM PRFLAVLVEN YQQEDGTIRV PDALIPYVGK
EILGHTA
//
