SYGB_DESAP
ID SYGB_DESAP Reviewed; 688 AA.
AC B1I1T4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Daud_0485;
OS Desulforudis audaxviator (strain MP104C).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Candidatus Desulforudis.
OX NCBI_TaxID=477974;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP104C;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL Submitted (OCT-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; CP000860; ACA59031.1; -; Genomic_DNA.
DR RefSeq; WP_012301620.1; NC_010424.1.
DR AlphaFoldDB; B1I1T4; -.
DR SMR; B1I1T4; -.
DR STRING; 477974.Daud_0485; -.
DR EnsemblBacteria; ACA59031; ACA59031; Daud_0485.
DR KEGG; dau:Daud_0485; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000008544; 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; Reference proteome.
FT CHAIN 1..688
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101271"
SQ SEQUENCE 688 AA; 75568 MW; 3129DB77C8E89F25 CRC64;
MAADLVLEIG TEEIPARFLP PALAELAEKG RALLAEYRLA YADLAAYGTP RRLTLYVRDL
AGDQAPLVQE IKGPPKKAAF DIDGVPTKAA LGFARSQGVA VEDLVTRAVG PVEYVYAVRQ
ETGRPAAEIL AELGPRLIGA LVFPRPMRWG DQDFRFVRPI RWILCVHGDR VIEFTVAGVR
SGPHTWGHRF LSAGRLLVTT AGDYFTLLEE NFVIVDPARR REMVWEQVRA AAAAESGTVA
DDPELLAEVA DLLEYPSAFC GCFPESYLEL PEPVLVTPMR EHQRYFPVRD GTGRLMPFFV
GVHNGTAEHL NLIRSGNEKV LRARLADAAF FFREDLEVPL PDRGPELKKV VFQESLGTMH
EKVERLTALA GYLSSALGLD ETERAQAHRA AVLSKNDLLT SMVYEFPELQ GIMGREYALR
AGEAPAVAEA IREQYLPAPG GEELPATRAG LVLALADRAD NLVGAFGMGV QPTGSQDPYA
LRRQALGICH LLLDTPAYLD LDDFFREAYA AYGGRLTVEA GEVAAQLADF FGQRLRVLFQ
DRGLSYGVVE AALAAGHADV RDAWERATAV ATFQSHPAFA DISTAFTRAN NLAKNAAGTR
VEPALFKDPV EHTLYQAFLQ VREQVEAQIA RRRYGAALAA LAELREPVDR FFDGVMVMVE
EAAVRENRLA LLRLVADLFK GIADLSKF