ID A0A1E5KVW8_9ENTE Unreviewed; 694 AA.
AC A0A1E5KVW8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
GN Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN ORFNames=BCR26_15230 {ECO:0000313|EMBL:OEH81995.1};
OS Enterococcus rivorum.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=762845 {ECO:0000313|EMBL:OEH81995.1, ECO:0000313|Proteomes:UP000095256};
RN [1] {ECO:0000313|EMBL:OEH81995.1, ECO:0000313|Proteomes:UP000095256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25899 {ECO:0000313|EMBL:OEH81995.1,
RC ECO:0000313|Proteomes:UP000095256};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEH81995.1}.
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DR EMBL; MIEK01000032; OEH81995.1; -; Genomic_DNA.
DR RefSeq; WP_069699069.1; NZ_MIEK01000032.1.
DR AlphaFoldDB; A0A1E5KVW8; -.
DR STRING; 762845.BCR26_15230; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000095256; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00255};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00255};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Reference proteome {ECO:0000313|Proteomes:UP000095256}.
FT DOMAIN 586..681
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 694 AA; 78846 MW; C3CCA1F57503EF3F CRC64;
MAKDLLLEIG LEEMPAHVVT PSRIQLEEKV IKFLDENNLS YESVQTFSTP RRLAIRVTQI
PEQQEDTEEE VKGPAKKIAL DAEGNWSKAA QGFVRGQGVS TDNIVFKEVN GVDYIFVTKF
TKGKSAMEVL KGLKQIITSL TFPVTMHWSD YDFEYIRPIH WIVALLDDQV IPFSVLDVVT
GAQSRGHRFL GDDIIFSHAN QYEEKLKEQF VIVDPLERKK MIVDQANVFA AEKNWTIDLD
EKLLEEVNNL VEYPTAFVGD FDEKYLSVPE EILITSMKEH QRYFAIHNEQ GMLMPHFIAV
RNGDSVHIEN VKKGNEKVLI ARLEDAEFFY SEDKKLSLED CVDKLKNVTF HEKIGTIYEK
MQRVGLIGQI IGKEVGLSDS ELEDLKRASE IYKFDLVTNM VGEFPELQGI MGEKYALLQG
EKPSVAQAIR EHYMPTASEG TLPESSIGAV LAIADKLDSV FSFFAVDMIP SGSNDPYALR
RQAYGIIRIV ENKGWDFPLV KLQLDIDEAV NADIAKFGIQ LKKGQAEVID FVKGRVRQLL
LTKNIRHDVI DAVISAEQKD LSKLFSSASI LKGHIQDKDF RPSVEALTRV INLAKKATET
VDENKLIINP DLFENDAEKE LYREVSEIAN HFDENSIVDN YNALVSLRPY IENYFENTMV
MVDDEKIKEN RLKQLIQIAK MARSIASLDL LIVK
//
