SYGB_RICFE
ID SYGB_RICFE Reviewed; 664 AA.
AC Q4UJU2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=RF_1346;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(2005).
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; CP000053; AAY62197.1; -; Genomic_DNA.
DR RefSeq; WP_011271646.1; NC_007109.1.
DR AlphaFoldDB; Q4UJU2; -.
DR SMR; Q4UJU2; -.
DR STRING; 315456.RF_1346; -.
DR EnsemblBacteria; AAY62197; AAY62197; RF_1346.
DR KEGG; rfe:RF_1346; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_1_5; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000008548; 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.
FT CHAIN 1..664
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_0000274898"
SQ SEQUENCE 664 AA; 75293 MW; 90A7C83087E3FD52 CRC64;
MSELLLELFS EEIPAFMQKN AEEGYLNIFT KIFEENEIFA KVQAFAGPRR ITLYATHLPK
VTLPKETEIK GPSIDAPEAA INGFCKAHNV SKLELSTKLI NNQLYYFFVK KTEEREIKEI
LPEIIIEAIN KYSWAKSMFW GDYKIKWIRP LRNILCIFDG EVLPLQFGHL TANNIAYGHR
YRLTDNKKLE VTDFEDYKNK LSENHVILER TKREEIIKTG LLELANSRNL NIKEDNRLIE
EVAGLSEFPV VLLGKIPQKF LELPKEVLIS SMRTHQKYFC LFDKEGNFAQ YFLFVSNGRF
ANAELVIKGN EKVLSARLSD ALYFYKQDIA KTLESRLGKL EAVTFHAKLG NLREKVERVA
KICSYTALDN TDLITAAKLC KSDLVSEMVG EFPDLQGIMG YYYAKHEGLG EEVAAAIKDH
YKPQGLSDNV PGGNAALLAL ADKVDSLVGL MIAGEAPTGS GDPYALRRQA LGIIRIILEN
KLELNLNDLI IFSLKLYGNS ADKDLITSFF EERAKFYFKN DYDIALINAA LDLNLVDTKF
KLDSLKEFLV EDAGKQLLNA YKRASNIIDG QKITGLVDAS LFSTQPEKEL FEVMQKISPQ
VTSSISDKDY NKALNLLSFL LTPITSFFDN VLVNDPDPKI AENRLSLLHN ICELFDKVAK
FCRL