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Database: UniProt
Entry: R4WW71_9BURK
LinkDB: R4WW71_9BURK
Original site: R4WW71_9BURK 
ID   R4WW71_9BURK            Unreviewed;       366 AA.
AC   R4WW71;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000256|HAMAP-Rule:MF_00254,
GN   ECO:0000313|EMBL:BAN22172.1};
GN   ORFNames=BRPE64_ACDS04180 {ECO:0000313|EMBL:BAN22172.1};
OS   Caballeronia insecticola.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=758793 {ECO:0000313|EMBL:BAN22172.1, ECO:0000313|Proteomes:UP000013966};
RN   [1] {ECO:0000313|Proteomes:UP000013966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23833137; DOI=10.1128/genomeA.00441-13;
RA   Shibata T.F., Maeda T., Nikoh N., Yamaguchi K., Oshima K., Hattori M.,
RA   Nishiyama T., Hasebe M., Fukatsu T., Kikuchi Y., Shigenobu S.;
RT   "Complete Genome Sequence of Burkholderia sp. Strain RPE64, Bacterial
RT   Symbiont of the Bean Bug Riptortus pedestris.";
RL   Genome Announc. 1:340-344(2013).
RN   [2] {ECO:0000313|EMBL:BAN22172.1, ECO:0000313|Proteomes:UP000013966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RPE64 {ECO:0000313|EMBL:BAN22172.1};
RX   PubMed=29863457; DOI=10.1099/ijsem.0.002848;
RA   Takeshita K., Tamaki H., Ohbayashi T., Meng X.-Y., Sone T., Mitani Y.,
RA   Peeters C., Kikuchi Y., Vandamme P.;
RT   "Burkholderia insecticola sp. nov., a gut symbiotic bacterium of the bean
RT   bug Riptortus pedestris.";
RL   Int. J. Syst. Evol. Microbiol. 68:2370-2374(2018).
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:0000256|ARBA:ARBA00000201,
CC         ECO:0000256|HAMAP-Rule:MF_00254};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00254}.
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DR   EMBL; AP013058; BAN22172.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4WW71; -.
DR   STRING; 758793.BRPE64_ACDS04180; -.
DR   KEGG; buo:BRPE64_ACDS04180; -.
DR   PATRIC; fig|758793.3.peg.417; -.
DR   HOGENOM; CLU_057066_1_0_4; -.
DR   Proteomes; UP000013966; Chromosome 1.
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   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   NCBIfam; TIGR00388; glyQ; 1.
DR   PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00254};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00254}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00254};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00254};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00254}.
FT   REGION          337..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   366 AA;  42036 MW;  5F705CFADF31C5D1 CRC64;
     MFQHFGRLSE SRRHDDGRAP HKAIMLTFQQ IILTLQSYWN DKGCALLQPI DMEVGAGTSH
     VHTFLRAIGP EPWRAAYVQP SRRPKDGRYG ENPNRLQHYY QYQVVLKPAP EDILDLYLGS
     LEALGFDLKQ NDVRFVEDDW ENPTLGAWGL GWEVWLNGME VTQFTYFQQA GGIDCKPVLG
     EITYGLERLA MYLQKVENVY DLVWTEWEED GPDGRVLRRL TYGDVYHQNE VEQSTYNFEH
     ANVDLLFTFF KSYEEEAKKM IDAKLALPAY ELVLKAGHTF NLLDARGAIS VTERAAYIGR
     IRALSRLVAQ TYYESREALG FPMLGNPVRG DRDLITDEQE AQRPAWAPPL RVESAPPGET
     RNNEQV
//
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