SYGB_MANSM
ID SYGB_MANSM Reviewed; 689 AA.
AC Q65R47;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-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=MS1956;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU38563.1; -; Genomic_DNA.
DR RefSeq; WP_011201114.1; NC_006300.1.
DR AlphaFoldDB; Q65R47; -.
DR SMR; Q65R47; -.
DR STRING; 221988.MS1956; -.
DR EnsemblBacteria; AAU38563; AAU38563; MS1956.
DR KEGG; msu:MS1956; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000000607; 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..689
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006378"
SQ SEQUENCE 689 AA; 76139 MW; 6169C1A01367EC2E CRC64;
MTTQNFLAEI GTEELPPKAL KKLATAFAEN VENELNQAGL TFEKVQWFAA PRRLAVKVLN
LATSQPTKEI EKRGPAVSAA FDAEGKPTKA AEGWARGCGI TVEQAERLAT DKGEWLVHRA
TIEGQPTKNL MLDIVTRSLA NLPIPKMMRW GDKTEQFVRP VHTVSLLLGG ELIEGEILGI
ASGRTIRGHR FLGEAEFQIA HADEYPQILK DKGSVIADFN ERRAIILADS QAKASALGGV
ADIEDDLLDE VTSLVEFPNV LTATFEERFL AVPAEALVYT MKGDQKYFPI YDKNGKLLPH
FIFVSNINPT DPTPIIEGNE KVVRPRLSDA EFFFNTDKKQ RLEDLLPRLE TVLFQQQLGT
LLDKTKRIQA LAGEIATQIG ADKAKAERAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
GEDEEVAVAL NEQYMPRFAG DNLPNSLVAS SVALADKFDT LTGIFGIGQA PKGSADPFAL
RRAALGALRI IVEKNLPLDL AEIVKKSTAL FADRLTNQNV VDDVVDFMLG RFRAWYQDEG
IAVDVIQAVL ARRPTKPADF DARVRAVSHF RTLDSAEALA AANKRVSNIL AKIEGEISSK
IDRTLLLEPE EKALAEQVLA LQSELAPLFA KGEYQPALDR LAGLREVIDN FFDKVMVNAE
DEKLRQNRQA ILNTLRNLFL QVADISLLQ