SYGA_COXBU
ID SYGA_COXBU Reviewed; 319 AA.
AC P94616;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Glycine--tRNA ligase alpha subunit;
DE EC=6.1.1.14;
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit;
DE Short=GlyRS;
GN Name=glyQ; OrderedLocusNames=CBU_1913;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RA Willems H., Jaeger C.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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;
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; Y10435; CAA71456.1; -; Genomic_DNA.
DR EMBL; AE016828; AAO91404.1; -; Genomic_DNA.
DR RefSeq; NP_820890.1; NC_002971.3.
DR RefSeq; WP_005769976.1; NZ_CCYB01000002.1.
DR AlphaFoldDB; P94616; -.
DR SMR; P94616; -.
DR STRING; 227377.CBU_1913; -.
DR EnsemblBacteria; AAO91404; AAO91404; CBU_1913.
DR GeneID; 1209826; -.
DR KEGG; cbu:CBU_1913; -.
DR PATRIC; fig|227377.7.peg.1897; -.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_057066_1_0_6; -.
DR OMA; SYYQFQV; -.
DR Proteomes; UP000002671; 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 CDD; cd00733; GlyRS_alpha_core; 1.
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; Reference proteome.
FT CHAIN 1..319
FT /note="Glycine--tRNA ligase alpha subunit"
FT /id="PRO_0000072835"
SQ SEQUENCE 319 AA; 36397 MW; FF52579A9F0787F8 CRC64;
MKSSHPVNFQ QMILALQEYW ASQGCVLLQP FDMEVGAGTF HPATFLRAIG PEPWRAAYVQ
PSRRPTDGRY GDNPNRTQHY YQFQVVLKPS PDDIQDIYLG SLKALGIDPL THDIRFVEDN
WEAPTLGSWG VGWEVWQDGM EITQFTYFQQ IGGLECKPVT GEITYGLERL AMFLQGIDNM
FDLVWTEGPN GRVTYGQIFQ QNEVEMSAYN FEYANVEALF NFFDFYEKEA SQLIEVHLPL
AAYEMVLKAS HTFNLLDARQ AISVTERQRF ILRVRKLAQA VAEAYYSARE KLGFPMLEEI
SSSSSRVLPL AGNDRVKGC