SYGB_ACTPJ
ID SYGB_ACTPJ Reviewed; 689 AA.
AC B0BSX5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=APJL_1839;
OS Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=434271;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL03;
RX PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA Zhao G.-P., Chen H.;
RT "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT serotype 3 prevalent in China.";
RL PLoS ONE 3:E1450-E1450(2008).
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; CP000687; ABY70389.1; -; Genomic_DNA.
DR RefSeq; WP_012263395.1; NC_010278.1.
DR AlphaFoldDB; B0BSX5; -.
DR SMR; B0BSX5; -.
DR EnsemblBacteria; ABY70389; ABY70389; APJL_1839.
DR KEGG; apj:APJL_1839; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000008547; 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 SMART; SM00836; DALR_1; 1.
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_1000101260"
SQ SEQUENCE 689 AA; 76151 MW; 64BF44344AAF6D62 CRC64;
MTTQNFLAEI GTEELPPKAL KKLATAFAEN VENELNQAGL SFEKVEWFAA PRRLAVKALG
LATAQPSKKI EKRGPAVSAA FDADGKPTKA AEGWARGCGI SVEQAERLAT DKGEWLVHRA
VIEGQPTKNL LVDIISRSLA NLPIPKMMRW GDKTEQFVRP VHTVTLFFGG ELIEGEILGV
KIANVVRGHR FLGEREFTIS HADEYLTALR EKGSVIADFN ERKALILAKS QEKATALGGV
ADIEEDLLDE VTSLVEFPNV LTAKFEERFL AVPAEALVYT MKGDQKYFPI YDKDGKLLPH
FIFVSNINPE DPTAIIEGNE KVVRPRLTDA EFFFKTDLKQ RLEDRLPRLE TVLFQQQLGT
LRDKTARIEA LAGEIAAQIG ADKAKAERAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
GEDEEVAVAL NEQYMPRFAG DELPKSLVAC SVALADKFDT LTGIFGIGQA PKGSADPFAL
RRAALGSLRI IVEKNLPLDL EDLVRKSAAL FGDKLTNANV VDDVVDFMLG RFRAWYQDEG
IAVDVIQAVL ARRPTKPADF DARVRAVSHF RTLDSAEALA AANKRVSNIL AKVEGEISTE
IDRSLLVEAE EKALAEQVIS LQTELAPTFA NGEYQTALDR LASLRETVDS FFEKVMVNAE
DANLRRNRQA ILNNLRNLFL QVADISVLQ