SYGB_SYNC1
ID SYGB_SYNC1 Reviewed; 688 AA.
AC Q3A8N5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=Pcar_0599;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-2005) 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; CP000142; ABA87858.1; -; Genomic_DNA.
DR RefSeq; WP_011340299.1; NC_007498.2.
DR AlphaFoldDB; Q3A8N5; -.
DR SMR; Q3A8N5; -.
DR STRING; 338963.Pcar_0599; -.
DR EnsemblBacteria; ABA87858; ABA87858; Pcar_0599.
DR KEGG; pca:Pcar_0599; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_7; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000002534; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR PANTHER; PTHR30075; PTHR30075; 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..688
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006382"
SQ SEQUENCE 688 AA; 75602 MW; 4ED184E2B25A5304 CRC64;
MSAELFLEIG TEEIPAGFLP TAMADLERLI RKELETGRIG FETVRTFATP RRLVLAVTGV
ASGQARQEVT ASGPSVSVAF DADGNPTKAA LGFARSNGVE VSDLERRETD KGEYLFVSKV
VEGRPTGELL PEMLPRIIAA IPFKKSMRWK DLDIRFARPM HWIVALFDGQ VVPFSYGNLT
SGNLSYGHRF MAPDAFEVSS LEQYLVEAEK HFVIVDPVKR RQIISDQLAE VVGRCGGKLN
PDDDLLDEVA FLVEYPAAVM GGFEDSYLQL PPELLITVMR EHQRYFTVVD DSGKLLPRFI
TISNTRAEDL TVVQQGNERV LRARLSDAMF FWNEDRKVKL ESRLDALKNV VYQAKLGTSY
EKVMRFKTLA VELAQQQVPE VVELTERAAS LAKCDLETGM VFEFTELQGV MGREYALLDG
EDPRVARAIF EHYLPVQAGG ELPGDDVGAF VSIADKIDSI CGCFGVGLIP TGTADPFALR
RSAIGILNII LDRGYRLSLP ALVERSLGLL ADKLTRPATE VAADVLEFLR LRFFNMLTAQ
GLPNDVVDAV LSAAFEDPVD ALQRVKGLAS FREEGEFEAL AVTFKRVVNI VKGGVDTSVD
SALFEADCEA GLFDALQNVT GRFEQFVAEG AYLDALRTVG GLRSPVDALF EGVMVMSPDE
AVKTNRLALL TAVARLFQGI ADFSKIAA