SYGB_RICCN
ID SYGB_RICCN Reviewed; 664 AA.
AC Q92G11;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 3.
DT 25-MAY-2022, entry version 106.
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=RC1316;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL03854.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006914; AAL03854.1; ALT_INIT; Genomic_DNA.
DR PIR; D97864; D97864.
DR RefSeq; WP_010977873.1; NC_003103.1.
DR AlphaFoldDB; Q92G11; -.
DR SMR; Q92G11; -.
DR EnsemblBacteria; AAL03854; AAL03854; RC1316.
DR KEGG; rco:RC1316; -.
DR PATRIC; fig|272944.4.peg.1510; -.
DR HOGENOM; CLU_007220_2_1_5; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000000816; 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_0000072923"
SQ SEQUENCE 664 AA; 75585 MW; F9AACE0207FA1E10 CRC64;
MSELLLELFS EEIPAFMQKN AEEGYLNIFT KIFEENEIFA KVQVFVGPRR ITLHATHLPK
ITLPKEEEIK GPSIEAPEAA INGFCKAHNV SKLELPTKLI SNQLYYFFVK KTEEREIKEI
LPEIIIEAIN KYSWAKSMFW GDYKIKWIRP LRNILCIFDG EILPMQFGHL TANNITYGHR
LTDNKKLEVT DFEDYRNKLL ENHVILERAK REAIIKTGLL ELASSHELII KEDNRLVEEV
VGLSEFPVVL LGKIPQKFLE LPKEVLISSM RTHQKYFCLF DKTGNFTPYF LFVSNGRFTN
AELVIQGNEK VLSARLSDAL YFCKQDIAKT LESRLGQLEA VTFHAKLGNL REKIERITDI
CNYIAPNNKD LITAARLCKS DLVSEMVGEF PDLQGIMGYY YAKHEGLNAE IAAAIRDHYK
PQGLSDNLPS GNAALLALAD KLDSLVGLMI AGETPTGSGD PYALRRQALG IIRIILENKL
ELNFNDLINF SINLYKDSSD ENKNLIISFF EERAKFYFKN DYDIALINAV LDLNLVDTNF
KLDALKEFLI EDAGKQLLNA YKRASNIIGD QKITGLVDAS LFSTQPEKEL FEVIQKISPQ
IIDSIADKDY KKALNLLSSL LTPITSFFDN VLVNDSDPKI AQNRLSLLQN ICELFDKVAK
FNRL