SYGB_RHIE6
ID SYGB_RHIE6 Reviewed; 704 AA.
AC B3PRI2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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};
GN OrderedLocusNames=RHECIAT_CH0000980;
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652;
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) 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; CP001074; ACE89965.1; -; Genomic_DNA.
DR RefSeq; WP_012482873.1; NC_010994.1.
DR AlphaFoldDB; B3PRI2; -.
DR SMR; B3PRI2; -.
DR EnsemblBacteria; ACE89965; ACE89965; RHECIAT_CH0000980.
DR KEGG; rec:RHECIAT_CH0000980; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_1_5; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000008817; 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; 2.
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.
FT CHAIN 1..704
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101319"
SQ SEQUENCE 704 AA; 77176 MW; AD93C3C49DEF3B0C CRC64;
MPNLLLELRS EEIPARMQRK AAGDLKKLVT DALVEAGLSY EGAREYWTPR RLALDIHGLT
ARSADVREER KGPRTDANEK AIEGFLRGAG LSSVSEAQVV SDPKKGDFYV AVISKPGRAT
EEIVAEVMPG IIRDFPWPKS MRWGKASSKS GALRWVRPLQ SIVCTFGPEH EETTVIPFEI
DGITASNITY GHRFHAPEAI TVRRFDDYAA SLEKAKVILD AERRKDIILH DARDIAFANG
LELVEDEGLL EEVSGLVEWP QVLMGSFEED YLSIPSEIIR LTIKTNQKCF VTRKQGEDTL
SNRFILVSNI QAHDGGKEIV HGNGKVVRAR LSDALHFWKR DQGNLPDLET LAASAAKFGL
DLQKPLDQRM AKLDALDVTF HAKLGTQGAR VARIRALAKE LAAITGADPA LTDRAAVLAK
ADLRTEAVGE FPELQGLMGR KYAVLQGENA SVAAAVEDHY KPQGPSDRVP EDKVAITLAL
ADKLDTLTGF WAIDEKPTGS KDPFALRRAA LGVVRILLER RVRLPLLATT RDGDLLSFFH
DRLKVYLRDQ GARYDLIDAV LTPDADDLLM VARRVEALTA FITSEDGKNL LAGTKRATQL
LAAEEKKGTV IADGVSPALL KLDAEKELFA AISSASKDAA DAVAGEDFRS AMEALSKLRG
PVDRFFEEVL VNDEDAAIRA NRLALLRLIR EATGTVADFS KISG