ID   SYGB_HISS2              Reviewed;         688 AA.
AC   B0UWA9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=HSM_1792;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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; CP000947; ACA31576.1; -; Genomic_DNA.
DR   RefSeq; WP_012340895.1; NC_010519.1.
DR   AlphaFoldDB; B0UWA9; -.
DR   SMR; B0UWA9; -.
DR   STRING; 228400.HSM_1792; -.
DR   EnsemblBacteria; ACA31576; ACA31576; HSM_1792.
DR   KEGG; hsm:HSM_1792; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
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..688
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000078543"
SQ   SEQUENCE   688 AA;  75414 MW;  FF8E89945D5061EF CRC64;
     MTAQNFLAEI GTEELPPKAL KKLATAFAEN VEQELNQAGL AFEKVEWFAA PRRLAVKVLG
     LAEAQPSKQV EKRGPAVSAA FDAEGKPTKA AEGWARGCGI TVEQAERLAT DKGEWLVHRA
     VIEGQPTKNL LVGIIDKALA GLPIPKTMRW GDKTEQFVRP VHTVTLLFGA DLIEGEILGV
     ASGRTVRGHR FLGEREFSLD HADQYPQLLK ERGSVVADFN ERKALILATS QEKATALGGV
     ADIEEELLEE VTSLVEYPNV LTAKFEERFL AVPAEALVYT MKGDQKYFPI YDKDGKLLPH
     FIFVSNINPD DPSKIIEGNE KVVRPRLTDA EFFFKTDLKQ KLEDRLPRLE TVLFQQQLGT
     LRDKTARIEA LAGEIAAQIG ADQTKAKRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
     GEDEDVAVAL NEQYMPRFAG DTLPNSLVAC SVALADKIDT LTGIFGIGQS PKGSADPFAL
     RRAALGCLRI IVEKNLPLDL VDIVAKATAL FGDKLTNKNV VDEVVDFMLG RFRAWYESEG
     IAVDVIQSVL ARRPTKPADF DARVRAVSHF RTLDSAEALA AANKRVSNIL AKADIAIGEI
     DLGVCVESAE KTLAEAVIAL KGEVQPLIAQ GDYTAVLDKL ANLRQPIDAF FDGVMVNVEE
     QTLRQNRLAI LSTLQNLFLQ VADISVLQ