SYGB_METS4
ID SYGB_METS4 Reviewed; 704 AA.
AC B0UNU2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=M446_2759;
OS Methylobacterium sp. (strain 4-46).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4-46;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium sp. 4-46.";
RL Submitted (FEB-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; CP000943; ACA17197.1; -; Genomic_DNA.
DR RefSeq; WP_012332603.1; NC_010511.1.
DR AlphaFoldDB; B0UNU2; -.
DR SMR; B0UNU2; -.
DR STRING; 426117.M446_2759; -.
DR EnsemblBacteria; ACA17197; ACA17197; M446_2759.
DR KEGG; met:M446_2759; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_1_5; -.
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..704
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101302"
SQ SEQUENCE 704 AA; 75805 MW; 18A08E5B8757A769 CRC64;
MPDLLLELFS EEIPARMQRR AAEDLRKLVT DALVERGFLY EGAKAFSTPR RLALHVAGLP
VRGQDVREER KGPRVGAPEA AVQGFLKSAG LASLDQARVV ADPKKGEFYV AVIERPGRET
LDVLAEILPA IIRAFPWPKS MRWGAASAEP GALRWVRPLH AIVATFGPET ETPERVPFRV
DGIEAGFTTY GHRFLSPGPI EVRRFADYLP ALERAKVVLD ADRRKDIILH DARDLAFARG
LDLVEDEGLL EEVAGLVEWP VTLMGAFDAS FLDIPPEVIR ATIRANQKCF VLRAPAADPA
AKGRERLANA FILVSNLAAS DGGAAIVAGN ERVVRARLSD AKFFWETDRK IPLAERLPKL
DDIVFHEKLG TQAARVGRIA ALARAFAPVV GADPAEAERA ARLAKADLVT EMVGEFPELQ
GLMGRYYAEL QGEPEAVAAA IEEHYKPLGP GDRVPTGPVS VAVALADKLD TLVGFWSVDE
KPTGSKDPYA LRRAALGVIR LVLGAGARLP LLPALAAAAG GHGAAPGGFA ADLLGFFADR
LKVHLRDQGA RHDLIDAVFA LPGQDDLLLV VRRVEALGRL LDTEDGTNLL AGYRRAANIL
RIEEKKDGRA HDGAPDPARF ALPEETALAE ALAAARGAAE RAVAAEDFEG AMRALAGLRA
PVDAFFDKVT VNAEDPAMRE NRLALLGALR TATLAVADFS RIEG