ID A0A2U9TCJ4_9GAMM Unreviewed; 738 AA.
AC A0A2U9TCJ4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
GN Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN ORFNames=C9I47_0244 {ECO:0000313|EMBL:AWV05970.1};
OS Lysobacter maris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1605891 {ECO:0000313|EMBL:AWV05970.1, ECO:0000313|Proteomes:UP000249447};
RN [1] {ECO:0000313|EMBL:AWV05970.1, ECO:0000313|Proteomes:UP000249447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ9B {ECO:0000313|EMBL:AWV05970.1,
RC ECO:0000313|Proteomes:UP000249447};
RA Zhang X.-Q.;
RT "The complete genome of Lysobacter maris HZ9B, a marine bacterium
RT antagonistic against terrestrial plant pathogens.";
RL Submitted (MAY-2018) 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:0000256|ARBA:ARBA00000201,
CC ECO:0000256|HAMAP-Rule:MF_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
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DR EMBL; CP029843; AWV05970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9TCJ4; -.
DR KEGG; lmb:C9I47_0244; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000249447; 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 NCBIfam; TIGR00211; glyS; 1.
DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 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 SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00255};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00255};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Reference proteome {ECO:0000313|Proteomes:UP000249447}.
FT DOMAIN 633..736
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 738 AA; 80338 MW; 6F95958574C7B170 CRC64;
MSAPQAQHKR PLLVELGTEE LPVKALPGLA RAFFDGVVEG LRKRGIEVDG DDARPLYTPR
RLAVLLPGVA AEQPEQRNEV LGPYLNIALD ADGQPTRALQ GFAAKAGVDW QALERTSDNK
GERFVHRSVQ PGARTDALLP EILREAIAAM PIPKPMRWGG HDYGFARPVH WLVVLLGKDV
VDAELMGVRS DRMSRGHRFM HDKPVWFSTP DDYVESLRGA KVLVDPDERR ARIVAGVEAE
AKAVGGSARI DAGNLEEVNG LVEWPKAVRC GFEPEFLAVP AEALVATMEA NQKFFPLLDS
DGRLSEHFVG IANIESNDEA EVRKGYERVI RPRFADAKFF FVEDMKQGLA AMGEGLKQVT
YQAKLGSVAD KVARVAALAE AIAPQVGADP ALTRRAAELS KNDLQSRMVN EFPELQGIAG
RYYAMQDAAL DDLAHDDRVA VADAIDEAYR PRFGGDDIAL SPAGKVLAIA ERLDTLAGGF
AAGLRPTGNK DPFALRRNAL GLARTVIESG FDVDITELMR VSAAHASTAL LHAAAEKQQK
DAEDAERKGV KLADNQSGGM FLPNADALAN DLYDFILDRL RGYYADKGVP AQHFNAVAEL
KPKSLYDFDR RIDAVGTFAA LPEAEALAAA NKRIGNILKK ADIEVPGMED PALMNEPAER
ALAEAVEALY GETAEALRKG DYVTVLNHMA RVRPQVDAFF DAVMVNADDP AVRRNRLALL
RRLSERLGSV AAIEHLSI
//
