SYGB_RICAE
ID SYGB_RICAE Reviewed; 664 AA.
AC C3PLY4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
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=RAF_ORF1203;
OS Rickettsia africae (strain ESF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=347255;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ESF-5;
RX PubMed=19379498; DOI=10.1186/1471-2164-10-166;
RA Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B.,
RA Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.;
RT "Analysis of the Rickettsia africae genome reveals that virulence
RT acquisition in Rickettsia species may be explained by genome reduction.";
RL BMC Genomics 10:166-166(2009).
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; CP001612; ACP53974.1; -; Genomic_DNA.
DR RefSeq; WP_012720092.1; NC_012633.1.
DR AlphaFoldDB; C3PLY4; -.
DR SMR; C3PLY4; -.
DR EnsemblBacteria; ACP53974; ACP53974; RAF_ORF1203.
DR KEGG; raf:RAF_ORF1203; -.
DR HOGENOM; CLU_007220_2_1_5; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000002305; 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_1000204610"
SQ SEQUENCE 664 AA; 75601 MW; 7BC976A8CA2046E8 CRC64;
MSELLLELFS EEMPAFMQKN AEEGYLNIFT KIFEENEIFA KVQVFVGPRR ITLHATHLPK
ITLPKEEEIK GPSIEAPEAA INGFCKAHNV SKLELPTKLI SNQLYYFFVK KTEEREIKEI
LPEIIIEAIN KYSWAKSMFW GDYKIKWIRP LRNILCIFDG EILPMQFGHL TANNITYGHR
LTDNKKLEVT DFEDYRNKLL ENHVILERAK REAIIKTGLL ELANSHELII KEDNRLVEEV
VGLSEFPVVL LGKIPQKFLE LPKEVLISSM RTHQKYFCLF DKTGNFTPYF LFVSNGRFTN
AELVIQGNEK VLSARLSDAL YFCKQDIAKT LESRLGQLEA ATFHAKLGNL REKIERITDI
CNYIAPNNKD LITAARLCKS DLVSEMVGEF PDLQGIMGYY YAKHEGLNAE IAAAIRDHYK
PQGLSDNLPS GNAALLALAD KLDSLVGLMI AGETPTGSGD PYALRRQALG IIRIILENKL
ELNFNDLINF SINLYKDSSD ENKNLIISFF KERAKFYFKN DYDIALINAV LDLNLVDTNF
KLDALKEFLI EDAGKQLLNA YKRASNIIGD QKITGLVDAS LFSTQPEKEL FEVIQKISPQ
IIDSIADKDY KKALNLLSSL LTPITSFFDN VLVNDSDPKI AQNRLSLLQN ICELFDKVAK
FNRL