ID   SYGA_RICRO              Reviewed;         288 AA.
AC   B0BVK1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000255|HAMAP-Rule:MF_00254}; OrderedLocusNames=RrIowa_1542;
OS   Rickettsia rickettsii (strain Iowa).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=452659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Iowa;
RX   PubMed=18025092; DOI=10.1128/iai.00952-07;
RA   Ellison D.W., Clark T.R., Sturdevant D.E., Virtaneva K., Porcella S.F.,
RA   Hackstadt T.;
RT   "Genomic comparison of virulent Rickettsia rickettsii Sheila Smith and
RT   avirulent Rickettsia rickettsii Iowa.";
RL   Infect. Immun. 76:542-550(2008).
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_00254};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000766; ABY73261.1; -; Genomic_DNA.
DR   RefSeq; WP_012151423.1; NC_010263.3.
DR   AlphaFoldDB; B0BVK1; -.
DR   SMR; B0BVK1; -.
DR   STRING; 452659.RrIowa_1542; -.
DR   EnsemblBacteria; ABY73261; ABY73261; RrIowa_1542.
DR   GeneID; 45539786; -.
DR   KEGG; rrj:RrIowa_1542; -.
DR   eggNOG; COG0752; Bacteria.
DR   HOGENOM; CLU_057066_1_0_5; -.
DR   OMA; SYYQFQV; -.
DR   Proteomes; UP000000796; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00388; glyQ; 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..288
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000078533"
SQ   SEQUENCE   288 AA;  33209 MW;  C92C91E929235206 CRC64;
     MKKLSFQQII LTLQNYWQDY GCAILQPYDA YVGAGTFHPA TVLRCLGTKP WSVAYVQPSR
     RPGDSRYGMH PNRMQHYYQF QVILKPSPDN IQELYLKSLE CLGIDLKIHD IRFVEDDWES
     PTLGAAGLGW EVWCNGMEVS QFTYMQQIGG IECRPVAGEI TYGLERLALY IQGVDEVREL
     DWNGQVGEKA LKYGEVDFEA EWQFSKYNLE LADSEMLLRH FKDSEDQCER LIKANLPMPA
     YDECLKASHA FNQLNALGVI SVTERASYVL RVRHLARICC TKWLEMNK