SYGB_PSEMY
ID SYGB_PSEMY Reviewed; 684 AA.
AC A4XN72;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Pmen_0013;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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; CP000680; ABP82788.1; -; Genomic_DNA.
DR RefSeq; WP_011920371.1; NC_009439.1.
DR AlphaFoldDB; A4XN72; -.
DR SMR; A4XN72; -.
DR STRING; 399739.Pmen_0013; -.
DR PRIDE; A4XN72; -.
DR EnsemblBacteria; ABP82788; ABP82788; Pmen_0013.
DR KEGG; pmy:Pmen_0013; -.
DR PATRIC; fig|399739.8.peg.14; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
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..684
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006391"
SQ SEQUENCE 684 AA; 74341 MW; 639F5C38F18D11A0 CRC64;
MSAKDFLVEL GTEELPPKAL KSLGDAFLAG IEKGLKAAGL NYAASRVYAA PRRLAVLVEQ
LEEQQADRSM NLDGPPIQAA FDADGNPTQA ALGFARKCGV DIAEIDRSGA KLRFAQHIPG
QPAVNLLPTI VQDSLNDLPI PKRMRWAARR DEFVRPTQWL VMLFGDAVVD CEILAQKAGR
VSRGHRFHAN REVRISSPAN YAEDLRSAYV LADFAERREI ISRRVDELAA AEQGTAIVPP
ALLDEVTALV EWPVPLVCSF EERFLEVPQE ALISTMQDNQ KYFCLLDAGG KLLPRFITVA
NIESKDPAQI VSGNEKVVRP RLTDAEFFFK QDKKQKLEGF NQRLANVVFQ AQLGSVFDKA
QRVSALAGFI AREVGGDEAR AARAGLLSKC DLATEMVGEF PEMQGIAGYY YALNDGEPQD
VALALNEQYM PRGAGAELPS TLTGAAVAVA DKLDTLVGIF GIGMLPTGSK DPYALRRAAL
GVLRILIEKG LDLDLAAAVD FAVAQYAGKV KSDGLAAQVL EFIFDRLRAR YEDEGIEVAV
YQAVRAVNPT SPLDFDQRVQ AVQAFRKLPQ AEALAAANKR VSNLLSKAEG GVAAQVEAHY
FDNPSEFALH AAIQQADQAV QPLAAARQYN EALAKLASLR EPVDAFFEAV LVNAEDARVR
ANRYALLARL RGLFLGVADI SVLG