SYGB_RALPJ
ID SYGB_RALPJ Reviewed; 697 AA.
AC B2UFN5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=Rpic_0400;
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-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; CP001068; ACD25558.1; -; Genomic_DNA.
DR RefSeq; WP_009239103.1; NC_010682.1.
DR AlphaFoldDB; B2UFN5; -.
DR SMR; B2UFN5; -.
DR STRING; 402626.Rpic_0400; -.
DR EnsemblBacteria; ACD25558; ACD25558; Rpic_0400.
DR GeneID; 61387990; -.
DR KEGG; rpi:Rpic_0400; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_4; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
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.
FT CHAIN 1..697
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101318"
SQ SEQUENCE 697 AA; 75193 MW; E1A1F7B569324CC9 CRC64;
MSTLLIELLT EELPPKALAR LGEAFARGLF DGLSAQGLLE EGAAVEGFAT PRRLAASITG
ARRTAPDREL REKVLPVTIA FDAEGKPAAP LVKKLAALAK TVGVEVIAAE SLERGPDGKA
EALFYRYTAR GAVLADGLQT ALSQTIANLP IPKVMTYQRP NGENVQFVRP AHKLIALLDS
EVIPVSAFGL QSGNVTLGHR FLSAGEIVIQ DAASYASTLE SQGKVIAGYG KRKEAIRAEL
LKTAGADTVV MPEALLDEVN ALVEWPVVYP CHFEEAFLAV PQECLILTMQ TNQKYFALTD
AQGHLRNRFL IVSNIATDTP EAIIQGNERV VRPRLADARF FFEQDKKKPL ADRVPLLSRV
VYHNKIGTQL ERVSRLQAIA GQLAEKLGAD VAHASRGALL AKADLLTDMV GEFPELQGTM
GTYYARHDGE PDDVALACSE HYQPRFAGDA LPSTATGTVV ALADKLETLV GIWGIGLQPT
GEKDPFALRR HALGILRMLI EKPLALTIDD ALQIAAASFD GIAAVKPNLA AITDFLYDRL
RGYLKDKGYS TNEVEAVVSQ RPQRLDDIVA RLEAVRAFAA LPQAEALAAA NKRITNILKK
TDVAIGAVQP PLLKEDAERA LHQSVVSAEP QVHDAFARGD FTTALKTLAG LREAVDTFFD
GVMVMADDTA LRDNRLALLA ELHGLMNRVA DISKLAA