SYGB_POLNA
ID SYGB_POLNA Reviewed; 711 AA.
AC A1VJD8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Pnap_0444;
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2;
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(2009).
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; CP000529; ABM35766.1; -; Genomic_DNA.
DR RefSeq; WP_011799866.1; NC_008781.1.
DR AlphaFoldDB; A1VJD8; -.
DR SMR; A1VJD8; -.
DR STRING; 365044.Pnap_0444; -.
DR EnsemblBacteria; ABM35766; ABM35766; Pnap_0444.
DR KEGG; pna:Pnap_0444; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_4; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000000644; 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 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..711
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101315"
SQ SEQUENCE 711 AA; 76087 MW; 8C0CDD4104A35B78 CRC64;
MTTKNLLVEL FVEELPPKAL KKLGDAFAGV LAEQLKALGL ATAESVVTAY ASPRRLAAHI
SHVWLKADDK AVQQKLMPVS VGLDSAGHAT PALLKRLQAL GADLSDPVAA VAALKRAPDG
KAEALFYNSL VTGATLDTGL QKALEEAIAK LPIPKVMSYQ LETDCELPGW TSVNFVRPAH
GLVALHGSTV VPVKVLGLKA GNSTRGHRFE AAVDPVVLAD ADSYAVTLEI DGAVIASFAQ
RKAEIARQLA EAAAELGGGV QPIEDDALLD EVTALVERPN VLVCEFEKEF LDVPQECLIL
TMKANQKYFP LLDAAGKLTN KFLVVSNISP EDASFVIGGN ERVVRPRLAD AKFFFDQDRK
RTLASRVEGL GKVVYHNKLG TQGERTERVA EIAVKIAQLL EGDALAGKAG KAAWLAKADL
LTDMVGEFPE LQGTMGRYYA LHDGHSAEIA AAIEDHYKPR FAGDELPRNP VGVVVALADK
LETLVGMFGI GNLPTGDKDP FALRRHALGV IRMLVEKDLP LDLGALVGGA APVFGDKITD
ATPALLDFIY DRLSGSLREQ GYSAQEVDSV VSQKPQRLGD VPKRLAAVRA FAALPEAPAL
AAANKRIGNI LKKEALEVDP HVSELLLREA AEIALYAAMR DVVPTANAQF DTGDYTASLQ
TLAALRAPVD AFFDGVMVNA EELDLRLNRQ GLLKSLHNAM NRVADLSRLV A