SYGB_PHOPR
ID SYGB_PHOPR Reviewed; 689 AA.
AC Q6LW15;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 111.
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=PBPRA0055;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378663; CAG18510.1; -; Genomic_DNA.
DR RefSeq; WP_011216891.1; NC_006370.1.
DR AlphaFoldDB; Q6LW15; -.
DR SMR; Q6LW15; -.
DR STRING; 298386.PBPRA0055; -.
DR EnsemblBacteria; CAG18510; CAG18510; PBPRA0055.
DR KEGG; ppr:PBPRA0055; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000000593; Chromosome 1.
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; Reference proteome.
FT CHAIN 1..689
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006384"
SQ SEQUENCE 689 AA; 75892 MW; 1A843BDB8D8E2A41 CRC64;
MTERNFLIEL GTEELPPKAL RTLAEAFSSN FEAELKTAAL VHQGIEWFAT PRRLALKVTA
LATGQADSVV EKRGPAISAA FDAEGNPTKA AQGWARGNGI TVEQADTLKT EKGEWLLYKQ
EVKGKPAQEL LSGLAAAALA KLPIPKPMRW GNNEIQFIRP VKTLTMLLGD ELIEGNILGA
DSARIIRGHR FMGEAEFTID NADQYPAILE ERGKVMANYE ARKAIILEGA KKAALEVGGI
ADLEDELVEE VTSLVEWPVV LTASFEENFL NVPTEALVYT MKGDQKYFPV YDAEGNLIPK
FIFVTNIESK DPRQIIEGNE KVVRPRLADA EFFFKTDRKR PLVDRLPELE KAIFQKQLGT
IKDKTDRITE LAGYIAEQIG ADVTNAKRAG LLAKCDLMTS MVFEFTDTQG VMGMHYARHD
GEAEDVALAL YEQYMPRFAG DKLPSTGVSA AVAMADKIDT LVGIFGIGQA PKGSDPFALR
RAALGVLRII VEKDYSLDLV DLIAKARAQF GDKLTNANVE DEVIDFMLGR FRAWYQDEGH
SVDVILAVLA LRPTQPADFD KRVKAVSHFR SLDAAESLAA ANKRVGNILA KFDGELPLAV
DSSLLLEDAE KALAEKVEAM IATLAPVFAE GNYQQALSEL ATLREPVDAF FDNVMVMADD
EKLKVNRLTM LNLLRNEFLK VADISLVQK