ID SYGB_AERS4 Reviewed; 689 AA.
AC A4STG3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 01-MAY-2013, entry version 47.
DE RecName: Full=Glycine--tRNA ligase beta subunit;
DE EC=6.1.1.14;
DE AltName: Full=Glycyl-tRNA synthetase beta subunit;
DE Short=GlyRS;
GN Name=glyS; OrderedLocusNames=ASA_4261;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A.,
RA Kimball J., Munholland J., Murphy C., Sarty D., Williams J.,
RA Nash J.H., Johnson S.C., Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights
RT into the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate
CC + glycyl-tRNA(Gly).
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family.
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DR EMBL; CP000644; ABO92185.1; -; Genomic_DNA.
DR RefSeq; YP_001143933.1; NC_009348.1.
DR ProteinModelPortal; A4STG3; -.
DR STRING; 382245.ASA_4261; -.
DR EnsemblBacteria; ABO92185; ABO92185; ASA_4261.
DR GeneID; 4998368; -.
DR KEGG; asa:ASA_4261; -.
DR PATRIC; 20794984; VBIAerSal2987_4226.
DR eggNOG; COG0751; -.
DR HOGENOM; HOG000264302; -.
DR KO; K01879; -.
DR OMA; GMHYARL; -.
DR ProtClustDB; PRK01233; -.
DR BioCyc; ASAL382245:GJJN-4247-MONOMER; -.
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:HAMAP.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:HAMAP.
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 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; Complete proteome; Cytoplasm;
KW Ligase; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1 689 Glycine--tRNA ligase beta subunit.
FT /FTId=PRO_1000006350.
SQ SEQUENCE 689 AA; 75145 MW; BC1CCED6F64DAA59 CRC64;
MAQHTFLVEI GTAELPPKAL RSLAEAFADN FKAELTKADL AFGDIEWFAS PRRLALKVHA
LASEQPSKSV EKRGPAVSQA FDAEGKPTKA AEGWARGNGI TVEQAERLVT DKGEWLVHTA
KVEGRPAKDL LGELVASALA KLPIPKMMRW GDKTIQFVRP VFTVTLLLDG ELVPAHILGI
DSARTIRGHR FMGEPEFTID NASQYPQILL EKGKVVADFM ARKAKIKADA EAAAAAFGGV
ADLDDALLEE VTALVEWPVV LTANFEEKFL AVPAEALVHT MKGDQKYFPV YDKNGKLLPK
FIFVTNIESK DPSQIISGNE KVVRPRLSDA EFFFKTDLKQ TLASRLPRLE TVLFQQQLGT
VKAKVERIET VAGFIAERIG ANVAQAKRAG LLSKCDLMTN MVGEFASTQG VMGMHYARHD
GEDEVVAVAL NEQYMPRFAG DALPSALEAC AVALADKLDT LAGIFGIGML PKGDKDPFAL
RRAAIGALRI MTEKQLDLDL VELVEEAVRV YGDKLTNKTV VTDVVDFMLG RFRAAYQDEG
IGADVVLAVL ARRPTRPLDF DRRVKAVSHF RSLDAALALA AANKRVSNIL AKVEGELPTA
VKPELLQDAA EKALATQVAE LQAELAPLFA AGDYQAALTR LAALREPVDT FFNEVMVMAD
DEALKANRLA LLNNLRNLFL QVADISLLQ
//
