ID   SYGB_SHESW              Reviewed;         689 AA.
AC   A1RDW4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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};
GN   OrderedLocusNames=Sputw3181_0006;
OS   Shewanella sp. (strain W3-18-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W3-18-1;
RG   US DOE Joint Genome Institute;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. W3-18-1.";
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; CP000503; ABM22859.1; -; Genomic_DNA.
DR   RefSeq; WP_011787429.1; NC_008750.1.
DR   AlphaFoldDB; A1RDW4; -.
DR   SMR; A1RDW4; -.
DR   KEGG; shw:Sputw3181_0006; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000002597; Chromosome.
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   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..689
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000006410"
SQ   SEQUENCE   689 AA;  75139 MW;  1A720DCB438BFA74 CRC64;
     MNFENLLIEL GTEELPPKSL RKLAESFLAN FTEELTKADL AFSSAVWYAA PRRLAINVTE
     LALAQADKIV EKRGPAVSSA FDAEGKPTKA AEGWARGNGI TVEQAERLVT DKGEWLVHNA
     KVEGVETKSL IAAMAQRALD KLPIPKPMRW GNNKTQFIRP VHTATILLGS ELIEGELLGI
     KSARTVRGHR FMGLKQFELA HADHYLADLK EKGKVIADYE SRKALIKADA EKAAAKIGGT
     ADIEDSLLEE VASLVEWPVV LTASFEEKFL SVPSEALVYT MKGDQKYFPV FDDAGKLLPN
     FIFVANIESK DPAQIISGNE KVVRPRLADA EFFFNTDKKH TLESRLPSLE TVLFQQQLGT
     LKDKVNRISA LAAFIAEQTG ANAVDAARAG LLSKTDLMTN MVMEFTDTQG TMGMHYARLD
     GETEAVAVAM EEQYKPKFSG DTVPSAGVSC AVALADKLDT LVGIFGIGQA PKGAADPFAL
     RRAAIGVLRI IVENKLPLDL VTLIAKAQEL HGTHLSNVNA SDEVLEFLMA RFRAWYQDKG
     IGVDVILAVL ARRPTRPADF DSRINAVSHF RSLEASGALA AANKRVSNIL AKVEGALPTT
     IDASLLTEAA EQALAAKLNE LQPQLAPLFA NADYQQALTL LAGLRESVDQ FFEDVMVMAD
     DEALKNNRLA LLNNLREQFL HVADISLLQ