ID   SYGB_HAES1              Reviewed;         688 AA.
AC   Q0I273;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=HS_0479;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(2007).
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; CP000436; ABI24756.1; -; Genomic_DNA.
DR   RefSeq; WP_011608636.1; NC_008309.1.
DR   AlphaFoldDB; Q0I273; -.
DR   SMR; Q0I273; -.
DR   STRING; 205914.HS_0479; -.
DR   EnsemblBacteria; ABI24756; ABI24756; HS_0479.
DR   KEGG; hso:HS_0479; -.
DR   eggNOG; COG0751; Bacteria.
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..688
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000006366"
SQ   SEQUENCE   688 AA;  75476 MW;  17DA8399EF8C15EF CRC64;
     MTTQNFLAEI GTEELPPKAL KKLATAFAEN VEQELNQAGL AFEKVEWFAA PRRLAVKVLG
     LAEAQPSKQV EKRGPAVSAA FDAEGKPTKA AEGWARGCGI TVEQAERLST DKGEWLVHRA
     VIEGQLTKNL LVGIIDKALA GLPIPKTMRW GDKTEQFVRP VHTVTLLFGA DLIEGEILGV
     ASGRTVRGHR FLGEREFSLD HADQYPQLLK ERGSVVADFN ERKALILATS REKATALGGV
     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 ADIVAKATAL FGDKLTNKNV VDEVVDFMLG RFRAWYESEG
     IAVDVIQSVL ARRPTKPADF DARVRAVSHF RTLDSAEALA AANKRVSNIL AKADIAIGEI
     DLGVCVESAE KTLAEAVLAL KGEVQPLIAQ GDYTAVLDKL ANLRQPIDAF FDGVMVNVEE
     QTLRQNRLAI LSTLQNLFLQ VADISVLQ