ID SYGB_HAMD5 Reviewed; 689 AA.
AC C4K460;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=HDEF_0612;
OS Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Hamiltonella.
OX NCBI_TaxID=572265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5AT;
RX PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT "Hamiltonella defensa, genome evolution of protective bacterial
RT endosymbiont from pathogenic ancestors.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(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; CP001277; ACQ67353.1; -; Genomic_DNA.
DR RefSeq; WP_015873177.1; NC_012751.1.
DR AlphaFoldDB; C4K460; -.
DR SMR; C4K460; -.
DR STRING; 572265.HDEF_0612; -.
DR GeneID; 66260483; -.
DR KEGG; hde:HDEF_0612; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR Proteomes; UP000002334; 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 NCBIfam; TIGR00211; glyS; 1.
DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 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..689
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000204606"
SQ SEQUENCE 689 AA; 77624 MW; E85132C5172DDD03 CRC64;
MTHQTFLVEI GTEELPPKSL RSLVESFAFY LTQELNKAHL DHGEVTWFAT PRRLAVKVAC
LSTIQKDQKI EKRGPAIAQA YDVDGNPTKA ATAWARSCGI SLDQAKSLVT DKGEWLLYSW
VLPGKSASSL LAEKVKIALS QLPISKLMSW GIHEAKFVRP VHTVTLLLGD ELISGIIFGV
NSNRKILGHR FMGEPSFIIE HADQYPQILL EKGKVMADFF LRKTQIKTDI EKAAEKIGAI
ADISDNLLEE VTSLVEWPVV HTAQFEKKFL EVPSEALVHT MKNDQKYFPV YNKSGQLMPY
FIFVANILSQ DPPQLIFGNE KVIRPRFADA QFFFETDLKQ SLEERLPSLK TILFQKELGT
LYEKVQRVQA LSGWIASQIG ANVEYSIKAG LLSKSDLMTN MVCEFPETQG IMGMHYARYH
HEPDEVARAI YEQYQPRFSG DNLPSTLVAC SVAIADKMDT LTGIFGINQL PKGDKDPFGL
RRAALGVLRI IVEKNLPLDL QTLISEAVRL YGNKLKNSNL IDQIIEFMLG RFRSWYQEAG
HGIDSIQAVL ARRPTKPADF NARIQAVTYF RTMNEARALC ASNKRVSNIL SQSLDIPKNS
IDTGLLKEPA EIELAQNILE LEKKLAPFFV AGLYKDALLE LVALREPLDI FFKQVMVMVP
DQDLRLNRLA LLNKLRALFL RVADISFLQ
//
