SYGB_EDWI9
ID SYGB_EDWI9 Reviewed; 689 AA.
AC C5B995;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=NT01EI_0014;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) 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; CP001600; ACR67275.1; -; Genomic_DNA.
DR RefSeq; WP_015869500.1; NC_012779.2.
DR AlphaFoldDB; C5B995; -.
DR SMR; C5B995; -.
DR STRING; 67780.B6E78_11250; -.
DR PRIDE; C5B995; -.
DR EnsemblBacteria; ACR67275; ACR67275; NT01EI_0014.
DR GeneID; 7959334; -.
DR KEGG; eic:NT01EI_0014; -.
DR PATRIC; fig|634503.3.peg.12; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000001485; 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..689
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000204604"
SQ SEQUENCE 689 AA; 76045 MW; 06D62496E4DA51C5 CRC64;
MTQQTFLVEI GTEELPPKAL RSLAQAFADN FRTELDNAGL AHGDIEWFAA PRRLALKVAA
LNAAQPDREI EKRGPAIAQA FDAEGKPTKA AEGWARGCGI SVDQAERLST DKGEWLLYRA
LQKGQRAQDL LPALVASALS RLPIPKLMRW GDSDTQFVRP VHTVTLLLGS ESIPATILGV
PSDRVIRGHR FMGEAEFTLD SADQYPQILL ERGKVIADYD ARKALIKRDA EAAAARIGGV
ADLSDSLLEE VTSLVEWPVV LTARFEEKFL AVPAEALVYT MKGDQKYFPV YDAAGKLLPN
FIFVANIDSK DAQQIIAGNE KVVRPRLADA EFFFKTDRKQ RLEDNLPRLE SVLFQQQLGS
LRDKTDRITA LAGWIAQQIG ADVNMATRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
GEAEEVAVAL NEQYMPRFAG DALPTSLVAC AVAIADKMDT LAGIFGIGQH PKGDKDPFAL
RRAALGVLRI VVEKKLPLDL LTLTQEAVRL YGDKLGNASV VDDVVEFMLG RFRAWYQEEG
HAVDTIQAVL ARRPTRPADF DARVRAVSHF RTLPEAATLA AANKRVSNIL AKSGDVLAEQ
VQAVLLKEPA EIRLAANLIT LQEKLAPLFA DGRYQEALVE LATLRQPVDD FFEQVMVMAD
DEQVRINRLT LLNKLRDLFL QVADISVLQ