SYGB_SHEB2
ID SYGB_SHEB2 Reviewed; 689 AA.
AC B8E3Q5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=Sbal223_0012;
OS Shewanella baltica (strain OS223).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=407976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS223;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA Tiedje J.;
RT "Complete sequence of chromosome of Shewanella baltica OS223.";
RL Submitted (DEC-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; CP001252; ACK44556.1; -; Genomic_DNA.
DR RefSeq; WP_012586336.1; NC_011663.1.
DR AlphaFoldDB; B8E3Q5; -.
DR SMR; B8E3Q5; -.
DR EnsemblBacteria; ACK44556; ACK44556; Sbal223_0012.
DR KEGG; sbp:Sbal223_0012; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000002507; 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..689
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197214"
SQ SEQUENCE 689 AA; 75062 MW; 95A66558094273D6 CRC64;
MNFENLLIEL GTEELPPKSL RKLAESFLAN FTEELSKADL AFSSAVWYAA PRRLAINVTE
LALAQADKVV EKRGPAVSSA FDAEGKPTKA AEGWARGNGI TVEQAERLVT DKGEWLVHNA
KVEGVETKSL IAAMAQRALD KLPIPKPMRW GNNKTQFIRP VHTATMLLGS ELIEGELLGI
KSARTVRGHR FMGLKQFELA HADHYLADLK EKGKVIADYE SRKALIKADA EKAAAKIGGT
ADIEDSLLEE VASLVEWPVV LTASFEEKFL AVPSEALVYT MKGDQKYFPV FDDAGKLLPN
FIFVTNIESK DPAQIISGNE KVVRPRLADA EFFFNTDKKH TLESRLPSLE TVLFQQQLGT
LKDKVNRISA LAAFIAEQTG ANAVDAARAG LLSKTDLMTN MVMEFTDTQG TMGMHYARLD
GETEAVAVAM EEQYKPKFSG DTVPSAGVSC AVALADKLDT LVGIFGIGQA PKGAADPFAL
RRAAIGVLRI IVENKLPLDL VDLIAKAQAL HGTNLSNANA SDEVLEFLMA RFRAWYQDKG
IGVDVILAVL ARRPTRPADF DSRINAVSHF RSLEASSALA AANKRVSNIL AKVEGALPTT
INASLLTEAA EQALAAKLNE LQPLLAPLFA NADYQQALTL LAGLRESVDQ FFEDVMVMAD
DEALKNNRLA LLNNLREQFL HVADISLLQ