ID   SYGB_DICT6              Reviewed;         689 AA.
AC   B5YES4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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}; OrderedLocusNames=DICTH_1203;
OS   Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12).
OC   Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=309799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35947 / DSM 3960 / H-6-12;
RX   PubMed=24558247; DOI=10.1128/genomea.00109-14;
RA   Coil D.A., Badger J.H., Forberger H.C., Riggs F., Madupu R., Fedorova N.,
RA   Ward N., Robb F.T., Eisen J.A.;
RT   "Complete Genome Sequence of the Extreme Thermophile Dictyoglomus
RT   thermophilum H-6-12.";
RL   Genome Announc. 2:0-0(2014).
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; CP001146; ACI19384.1; -; Genomic_DNA.
DR   RefSeq; WP_012548016.1; NC_011297.1.
DR   AlphaFoldDB; B5YES4; -.
DR   SMR; B5YES4; -.
DR   STRING; 309799.DICTH_1203; -.
DR   EnsemblBacteria; ACI19384; ACI19384; DICTH_1203.
DR   KEGG; dth:DICTH_1203; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_0; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000001733; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 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_1000101275"
SQ   SEQUENCE   689 AA;  80665 MW;  707082609D564D97 CRC64;
     MGKNFLLEIG TEEMPAHFID PAIRQMYDFS LEYFKNKKIS LESVKIWATP RRLVVYIENL
     GEKQEAQEEE IRGPAAHIGY KDGMWTEVAK RFVEQYGASL EDLHIEETPK GKYIFLRKVK
     EGMNTLEILP DYITSLLKSI RFPKMMKWGD VDFYFGRPIR WIVALYGDTE IEVEIAGVKS
     SRYSRPPRFL PQIPIEIRDA DSYLNVMREN YIIVDQEERK NEILKQINKI ANENSFILDY
     EDDLLKEVNY LVEYPTALLG EFDKKYLALP EVVLIITMEK KQRYFPLRDA DGNLTNKFIV
     IRNGTDNYKD IVIQGNEKVL KARLSDAEYY YHEDTKHPLE KYTEKLSGII FQEQLGTIKD
     KVERVRILVR EIANILGLSS EENKILERSV NLYKADLGTL MVSEYPELHG IMGRIYAKIS
     GEKDPIPEVI GEYIYPRTLD DRLPSNFLAS ILGIADRIDS LTGYFALDLF PTGSEDPIGL
     RRISGGLLRL LLESSLKLNL RNLFVKSFEI YNFGEKYPLS QIDKGMGFIG QRLRNLLLDR
     YSIDIVDAVM EVGYDEMWRL KRRLDFISKF KEKESYEKLK KALNRLYRIL PKDFTPKEVS
     ENLLSSPFEK KLYEDYLKIK NEIFNDILEG NYEVLLSYDF LNEFSDDIEK FFDNVLVMSP
     NEDERINRLS LLSLIKLLFW EILDWSRLS