SYGB_ACIAC
ID SYGB_ACIAC Reviewed; 708 AA.
AC A1TUT0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Aave_4177;
OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=397945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAC00-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL Submitted (DEC-2006) 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; CP000512; ABM34718.1; -; Genomic_DNA.
DR RefSeq; WP_011797192.1; NC_008752.1.
DR AlphaFoldDB; A1TUT0; -.
DR SMR; A1TUT0; -.
DR STRING; 397945.Aave_4177; -.
DR EnsemblBacteria; ABM34718; ABM34718; Aave_4177.
DR KEGG; aav:Aave_4177; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_4; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000002596; 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..708
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101252"
SQ SEQUENCE 708 AA; 75937 MW; 8E7ED29582814D80 CRC64;
MTHPNLLVEL FVEELPPKAL QKLGDAFAGV LLAQLQAQGL ASAASRVTAY ASPRRLAAHV
TEVAPQAADK AVSQKLMPVT VGLDASGNAT PALLKKLAAL GADASAVPGL RRAPDGKAEA
LFLDSTVRGA TLSEGLQKAL QESVAKLPIP KVMRYQLSSG CEQPGWTSVS FVRPAHGLVA
LHGTEVLLSV SVLGLTAGNA THGHRFEAAV DPVVIRSADT YAQQLAEEGA VIAAFADRRA
EIARQLQAAA EQVGGGVRPI QDDALLDEVT ALVERPNVLV CEFEKQFLDV PQECLILTMK
ANQKYFPLLD AEGRLTHRFL VVSNIRPDDA SAVVGGNERV VRPRLADAKF FFDQDRKKTL
ESRVASLAKV VYHNQLGTQG ERVERVRAIA RAIAQQIGDV ELARQADQAA QLAKADLVTD
MVGEFPELQG TMGRYYAQAD GLPAEVADAI EDHYKPRFAG DTLPRGDVGV VVALADKLET
LVGMFGIGNL PTGDRDPFAL RRHALGVIRM LVEKELPLDL ETLLHSALPA FGDKIQDPTA
SLADFIYDRL AGSLREQGYS AQEVDAVLAL RPQRLALVGK QLAAVRAFAA LPEAPALAAA
NKRVTNILKK AGDVDAHVNP DLLREQAEKD LYAALQRFVP EADALFAAGD YTGSLQTLAV
LRAPVDAFFD DVMVNAEELD LRLNRQGLLQ SLHVAMNRVA DLSRLAVA