ID   SYGB_COXBR              Reviewed;         689 AA.
AC   A9NB99;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE            EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00255};
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE            Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00255};
GN   Name=glyS {ECO:0000255|HAMAP-Rule:MF_00255};
GN   OrderedLocusNames=COXBURSA331_A2116;
OS   Coxiella burnetii (strain RSA 331 / Henzerling II).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=360115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 331 / Henzerling II;
RA   Seshadri R., Samuel J.E.;
RT   "Genome sequencing of phylogenetically and phenotypically diverse Coxiella
RT   burnetii isolates.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC         tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC         COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00255};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00255}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00255}.
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DR   EMBL; CP000890; ABX77801.1; -; Genomic_DNA.
DR   RefSeq; WP_012220855.1; NC_010117.1.
DR   AlphaFoldDB; A9NB99; -.
DR   SMR; A9NB99; -.
DR   KEGG; cbs:COXBURSA331_A2116; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   TIGRFAMs; TIGR00211; glyS; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..689
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000078540"
SQ   SEQUENCE   689 AA;  77975 MW;  696416B5B4C5353A CRC64;
     MTTQDFLLEI GCEELPPRRL NQLSQALSQT IKSELEKADL SFENIHRYAT PRRLAVLVNN
     LALQQPQRKI ERQGPSVKAA FDKDQTPTLA CFGFAQSCGV STAQLKVKKT KKGEFIYCEI
     EQPGQNTLDL LPNIIQSALK QLPTPKAMRW GDHKEFFVRP VHWIILMLGK DLVPATLLGK
     MASCETRGHR FHHPKNILVT KPDDYQKLLL THGMVIADFE KRREKIRDLI QKAASEKGEA
     IIDEGLLEEV TGMVEWPVIL VGNFKAEFLE LPPEVLITTM KVHQRTFPIK NKNGDLLPYF
     IIVSNIESKN PKRVIVGNER VINARLADAS FFYDNDLRTS LENRLPKLGD VIFQRQLGTL
     ADKARRIEKL AAFIAKQINI DEQLAARAGL LSKCDLVSEM VYEFPTLQGI MGYYYAFHDK
     EPPLVAEAIK EHYLPRFSGD QLPRNLLSPC VAVADRIDTI IGIIGINKSP TGDKDPFALR
     RAALGILRIL IEKELSLDLF ALLNEAKNNY AVELPNVNVV NQSFDFIIER LRAWYLEKEV
     PASVFMAVLA SHPDDPLDFD RRIKAVQHFQ TLPEADALAA ANKRVSNILK KQAAELKSKT
     IDHSLFDSDA EHLLADQLKE RAELVNNLYK KADYTKALSE LASLKEPIDI FFDKVMVMVD
     DKEKRENRLA LLSSLQQLFS QIADISLLS