SYGB_ACISJ
ID SYGB_ACISJ Reviewed; 720 AA.
AC A1W3F3;
DT 24-MAR-2009, 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}; OrderedLocusNames=Ajs_0528;
OS Acidovorax sp. (strain JS42).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX NCBI_TaxID=232721;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS42;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
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; CP000539; ABM40778.1; -; Genomic_DNA.
DR RefSeq; WP_011803987.1; NC_008782.1.
DR AlphaFoldDB; A1W3F3; -.
DR SMR; A1W3F3; -.
DR STRING; 232721.Ajs_0528; -.
DR EnsemblBacteria; ABM40778; ABM40778; Ajs_0528.
DR KEGG; ajs:Ajs_0528; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_4; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000000645; 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..720
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101258"
SQ SEQUENCE 720 AA; 78008 MW; 70922925A521CF86 CRC64;
MNHQNLLVEL FVEELPPKAL QKLGDAFAGV LLEQLQAQGL TSAHSQLTAF ASPRRLAAHI
TEVLPAAADK AVSQKLMPVA VGLDASGQPT PALLKKLTAL GADAASVPQL KRVHDGKAEV
LFFESMAKGA LLADGLQKAL DEAIAKLPIP KVMRYQLQDG WTSVHFVRPA HGLVALHGTQ
VLVGVQALGL TAGNTTHGHR FEASVDPVVI QSADSYAEQL RSEGAVIASF AERRAEIARQ
LQAAADRVGG GVRPIEDAAL LDEVTALVER PNVLVCEFEK EFLAVPQECL ILTMKANQKY
FPLLDAEGKL THQFLVVSNI SPQDASAVIQ GNERVVRPRL ADAKFFFDQD RKKTLVSRVD
QLAKVVYHNK LGTQGERVER VRHIAKAIAT QLFTALAQGN AALDSQEGEI AQDYLLTCVD
NAALLAKTDL VTDMVGEFPE LQGIMGGYYA VSDGLPDEVA HAIEDHYKPR FAGDALPREN
VGVVVALADK LETLVGMFGI GNLPTGDRDP FALRRHALGV IRMLVEKELP LDLDALLASA
VPAFGDKIED TSAQLADFIY DRLAGSLREQ GYSAQEVDAV IALRPQRLAL VPRQLEAVRA
FTQLEEAPAL AAANKRVTNI LKKAGEVDPH VNEELLQEPA EKDLYAALQR FVPEANAQFD
SGDYTASLQT LAVLRAPVDA FFDDVMVNAE ELALRLNRQG LLKKLHMAMN RVADLSRLAV