SYGB_ACIET
ID SYGB_ACIET Reviewed; 720 AA.
AC B9MCM4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=Dtpsy_0544;
OS Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Diaphorobacter.
OX NCBI_TaxID=535289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TPSY;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT "Complete sequence of Diaphorobacter sp. TPSY.";
RL Submitted (JAN-2009) 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; CP001392; ACM32024.1; -; Genomic_DNA.
DR RefSeq; WP_012655567.1; NC_011992.1.
DR AlphaFoldDB; B9MCM4; -.
DR SMR; B9MCM4; -.
DR STRING; 535289.Dtpsy_0544; -.
DR EnsemblBacteria; ACM32024; ACM32024; Dtpsy_0544.
DR KEGG; dia:Dtpsy_0544; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_4; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000000450; 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 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..720
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197183"
SQ SEQUENCE 720 AA; 77923 MW; 22FC6F12D3EBC93D CRC64;
MNHQNLLVEL FVEELPPKAL QKLGDAFAGV LLEQLQAQGL TSAHSQLTAF ASPRRLAAHI
TEVLPAAADK AVSQKLMPVA VGLDASGQPT PALLKKLAAL GADAASVPQL KRVHDGKAEV
LFFESMAKGA LLADGLQKAL DEAIAKLPIP KVMRYQLQDG WTSVHFVRPA HGLVALHGSE
VLVGVQALGL TAGNTTHGHR FEASVDPVVI QSADSYAEQL RSEGAVIASF AERRAEIARQ
LQAAADRVGG GVRPIDDDAL LDEVTALVER PNVLVCEFEK DFLAVPQECL ILTMKANQKY
FPLLDAEGKL THQFLVVSNI SPQDASAVIQ GNERVVRPRL ADAKFFFDQD RKKTLVSRVD
QLAKVVYHNK LGTQGERVER VRHIAKAIAT QLFTALAQGN AALDSQEGEI AQDYLLTCVD
NAALLAKTDL VTDMVGEFPE LQGIMGGYYA VSDGLPDEVA HAIEDHYKPR FAGDALPREN
VGVVVALADK LETLVGMFGI GNLPTGDRDP FALRRHALGV IRMLVEKELP LDLDALLASA
VPAFGDKIED TSAQLADFIY DRLAGSLREQ GYSAQEVDAV IALRPQRLAL VPRQIEAVRA
FATLEQAPAL AAANKRVTNI LKKAGEVDPH VNEELLQEPA EKDLYAALQR FVPEANAQFD
SGDYTASLQT LAVLRAPVDA FFDDVMVNAE ELALRLNRQG LLKKLHMAMN RVADLSRLAV