SYGB_XANC8
ID SYGB_XANC8 Reviewed; 698 AA.
AC Q4UP08;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=XC_4177;
OS Xanthomonas campestris pv. campestris (strain 8004).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=314565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8004;
RX PubMed=15899963; DOI=10.1101/gr.3378705;
RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT "Comparative and functional genomic analyses of the pathogenicity of
RT phytopathogen Xanthomonas campestris pv. campestris.";
RL Genome Res. 15:757-767(2005).
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; CP000050; AAY51215.1; -; Genomic_DNA.
DR RefSeq; WP_011039155.1; NC_007086.1.
DR AlphaFoldDB; Q4UP08; -.
DR SMR; Q4UP08; -.
DR EnsemblBacteria; AAY51215; AAY51215; XC_4177.
DR KEGG; xcb:XC_4177; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000000420; 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..698
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006421"
SQ SEQUENCE 698 AA; 75076 MW; D12853800813631B CRC64;
MSEQLPLLIE LGTEELPVKA LPGLAQAFFD GVLAGLEKRG VAVTRGDAKP LSTPRRLAVL
LPGVATEQPE QRSEVLGPYL NIALDAEGKP TRALAGFAAK AGIDWTALER TSDAKGERFV
HRAVTPGAQA AALLPEILRE AIAAMPIPKP MRWGAHEYAF ARPVQWLVLL FGDTVIPAEL
LGVRGDRITR GHRFMHDGDI ALAAPGDYID ALRAAHVLVD ADARRARIVE EVDAAARQAG
GSARISDDNL EQVVNLVEWP SAVLCSFERA FLAVPQEALI ETMEINQKFF PVLDDGGKLT
EQFIGIANIV SKDVAEVAKG YERVIRPRFA DAKFFFDEDL KQGLEAMGAG LASVTYQAKL
GTVADKVARV AALAEAIAPQ VGADPVQARR AAELAKNDLQ SRMVNEFPEL QGIAGRHYAK
AAGEPSEISL AIDEAYQPRF AGDDIALSPL GKVLAIAERL DTLAGGFAAG LKPTGNKDPF
ALRRNALGLA RTVIESGFDL DLPKLIDVGL ASLPDAVKPH ADRNTETVRA DLYDFILDRL
KGYYADKGVA ATHFNAVAEL KPASLYDFDR RIDAIGIFAT LPEAEALAAA NKRIRNILRK
VEGEIPGDID TTLLREPAEE ALAEAVEAAI GDTGDALHRH DYVAVLARLA RLRPQVDAFF
DGVMVNADDP QLRANRLALL KKLGDRLGSV AAIEHLSS