ID   SYGB_PARDP              Reviewed;         685 AA.
AC   A1AZF8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Pden_0540;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) 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; CP000489; ABL68652.1; -; Genomic_DNA.
DR   RefSeq; WP_011746885.1; NC_008686.1.
DR   AlphaFoldDB; A1AZF8; -.
DR   SMR; A1AZF8; -.
DR   STRING; 318586.Pden_0540; -.
DR   PRIDE; A1AZF8; -.
DR   EnsemblBacteria; ABL68652; ABL68652; Pden_0540.
DR   KEGG; pde:Pden_0540; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_1_5; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000000361; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..685
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101313"
FT   REGION          58..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   685 AA;  74632 MW;  F6485442E85060F1 CRC64;
     MPDLLIELFS EEIPARMQAR ARGDLKKLVT DGLVEAGLTY KSAGAFSTPR RLALAIEGLT
     AQSPTTREER KGPRTDAPEA ALEGFLRSTG LTREQLEARD DKKGQVWFAV VTKPGRPAAE
     IVAEVLERAI RDFPWPKSMR WGSGSLRWVR PLHSIICLLS DESGASVVPL EIEGIGAGNT
     TRGHRFMAPD EIAVSGFEDY AAKLRRARVM LDAAEREAAI RQEAANLAFA RGWEIVPDEG
     LLSEVAGLVE WPVPLMGAIE DRFLALPPEV LQTSMKEHQK FFSARNPKTG RIEGFVTVAN
     IETPDHGETI LKGNQRVLAA RLSDAAFFWE NDLREAKAGM ADWAEGLRSV TFQSKLGSQA
     DRIARIAALA LEIAPLVGAD ADQAEQAARI AKLDLRSAMV GEFPELQGIM GRYYALEAGL
     PEPVADAARD HYSPLGPSDA VPSAPVSVAV ALADKLDTLT GFWAIDEKPT GSKDPFALRR
     AALGVIRLLL VNGVRANLGQ TFAKARPDAD AADLLAFFHD RLKVHLRDQG VRHDIIDAVL
     SMPGNDDLVL LVNRATALSD VLKTEDGTNL LQGLKRAGNI LAQAEEMDGV EYSFGADPKF
     AETDEERTLF AALDKAEPAI REAVRLEDFQ AATQGIASLR APIDAFFEAV QINSDNQILR
     RNRLNLLSRI RDAGRLIADF GRIEG