SYGB_ACTP7
ID SYGB_ACTP7 Reviewed; 688 AA.
AC B3GZ55;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=APP7_1889;
OS Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=537457;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP76;
RA Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA Tegetmeyer H., Singh M., Gerlach G.F.;
RT "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL Submitted (JUN-2008) 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; CP001091; ACE62541.1; -; Genomic_DNA.
DR RefSeq; WP_005618275.1; NC_010939.1.
DR AlphaFoldDB; B3GZ55; -.
DR SMR; B3GZ55; -.
DR EnsemblBacteria; ACE62541; ACE62541; APP7_1889.
DR KEGG; apa:APP7_1889; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR BioCyc; APLE537457:APP7_RS09855-MON; -.
DR Proteomes; UP000001226; 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..688
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101259"
SQ SEQUENCE 688 AA; 75588 MW; 0ABF7BBF54E919E8 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 ARRPTRPADF DARVRAVSHF RTLDSAEALA AANKRVSNIL AKADVAIGEV
NPTACVEPAE KALAEAVLGL RTEVQPLIAK GEYTAVLDKL ASLRQPVDSF FDNVMVNAED
PALRQNRLAI LNTLQGLFLQ VADISLLQ