SYGB_DICTD
ID SYGB_DICTD Reviewed; 689 AA.
AC B8E0E8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, 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=Dtur_1319;
OS Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX NCBI_TaxID=515635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6724 / Z-1310;
RX PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT 6724 reveals a specialized carbohydrate fermentor.";
RL Front. Microbiol. 7:1979-1979(2016).
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; CP001251; ACK42593.1; -; Genomic_DNA.
DR RefSeq; WP_012583675.1; NC_011661.1.
DR RefSeq; YP_002353207.1; NC_011661.1.
DR AlphaFoldDB; B8E0E8; -.
DR SMR; B8E0E8; -.
DR STRING; 515635.Dtur_1319; -.
DR PRIDE; B8E0E8; -.
DR EnsemblBacteria; ACK42593; ACK42593; Dtur_1319.
DR KEGG; dtu:Dtur_1319; -.
DR PATRIC; fig|515635.4.peg.1364; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_0; -.
DR InParanoid; B8E0E8; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000007719; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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_1000197185"
SQ SEQUENCE 689 AA; 80746 MW; 78DB16219F7BB779 CRC64;
MGKNFLLEIG TEEMPAHFLD PAIKQIYDFS LNYFENQKIS FEDIKTWATP RRLVVYIKNL
SEKQESQEEE IRGPAAHVGY KNGVWTEVAK RFAEQYGASL EALYIKETPR GKYIFLKRIK
EGVNTLEILP DYAVSLLKNI RFPKMMKWGN VDFYFGRPIR WIVALYGSEE VKFEVAGVKS
SRYSRPPRFL PQTPIEIKDA DSYIDLMKEN YVIVDQNERK NEILRHIKEI ANSNSLTLSY
DEDLLEEVTY LVEYPTALLG QFDSKYLTLP EIVLIVTMEK KQRYFPLRDK EGNLINKFIV
IRNGTENYKE VVIQGNEKVL KARLADAEYY YNEDIRCPLE KYSEKLSGII FQEQLGTIKD
KVERVRILVR EIANILELST EEKEILERAV DLYKADLGTL MVSEYPELHG IMGSIYAKIS
GEREPIPQII GEYIYPRTLE DQIPKNPLST VLGIADRVDS LTGYFALDLF PTGSEDPIGL
RRISGGLLRL LLETDFKLNL RNLFMKSFEV YKFSDKCPIS QIEKGMLFIG QRLRNLLLDK
YPNDIVEAVM EVGYDELWKL KRRVDFIREF KEKDPYEKLK RALNRLYRIL PKDFSPKEIN
ENLFNSPFEK ELYRDYVKIN KEISKEILKG NYKVLLGYDF LKEFSDHIES FFDHVLVMSP
NEEEKLNRLS LLFAIKSLFW EVLDWSKLN