ID   SYGB_HAEAE              Reviewed;         285 AA.
AC   O30836;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Glycine--tRNA ligase beta subunit;
DE            EC=6.1.1.14;
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit;
DE            Short=GlyRS;
DE   Flags: Fragment;
GN   Name=glyS;
OS   Haemophilus aegyptius.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=197575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=F3031;
RA   Tondella M.L.C., Utt E.A., Mayer L.W., Quinn F.D.;
RL   Submitted (AUG-1997) 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;
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF018635; AAB70306.1; -; Genomic_DNA.
DR   AlphaFoldDB; O30836; -.
DR   SMR; O30836; -.
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-KW.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
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   SMART; SM00836; DALR_1; 1.
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..285
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072905"
FT   NON_TER         1
SQ   SEQUENCE   285 AA;  30957 MW;  034C4EE695DBB138 CRC64;
     EFTDTQGVMG MHYARHDGED EEVAVALNEQ YMPRFAGDEL PKSLVASAVA LADKFDTLTG
     IFGIGQAPKG SADPFALRRA ALGALRIIVE KNLPLDLEDL VKKSAALFGD KLANQNVVAD
     VVDFMLGRFR AWYQDEGIAV DVIQAVLARR PTRPADFDAR VRAVSHFRTL DSAEALAAAN
     KRVSNILAKA DAAIGEINLT VCVEQAEKAL AEAVLALRTE VQPLIEQGDY TTVLDKLANL
     RAPVDSFFDN VMVNAEDPAL RQNRLAILNT LQGLFLQVAD ISVLQ