ID A0A1B8VUW7_9BACI Unreviewed; 693 AA.
AC A0A1B8VUW7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=A7975_28020 {ECO:0000313|EMBL:OBZ08164.1};
OS Bacillus sp. FJAT-26390.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743142 {ECO:0000313|EMBL:OBZ08164.1, ECO:0000313|Proteomes:UP000092623};
RN [1] {ECO:0000313|EMBL:OBZ08164.1, ECO:0000313|Proteomes:UP000092623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-26390 {ECO:0000313|EMBL:OBZ08164.1,
RC ECO:0000313|Proteomes:UP000092623};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Z., Chen Q., Liu B.,
RA Zhu Y., Wang J., Liu G.;
RT "Bacillus sp. FJAT-26390.";
RL Submitted (MAY-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:OBZ08164.1}.
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DR EMBL; MAQX01000036; OBZ08164.1; -; Genomic_DNA.
DR RefSeq; WP_053376810.1; NZ_MAQX01000036.1.
DR AlphaFoldDB; A0A1B8VUW7; -.
DR Proteomes; UP000092623; 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:UP000092623}.
FT DOMAIN 593..674
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 693 AA; 77437 MW; DF49BE62A3607D82 CRC64;
MTRDLLLEIG LEEVPARFVR GAMNQLKDKM VKWLADSRIQ HGEVNVYATP RRIAVLIQEV
AEKQSDMNEE AKGPSRKIAQ DDQGNWSKAA LGFARSQGVE PEQLYFQELA GVEYVYANKS
SIGAETAAVL PEGLLSLITS MSFPKNMRWG SYELRFVRPI RWLVALFGQD VIPFEITGVQ
TGNVSRGHRF LGKEATVSAP AEYVERLREQ HVIADVSERE QLIVAQIDRL AKEKGWEIAI
KEDLLEEVLF LVEYPNVLFG GFDPAFLQIP QEVLITSMRE HQRYFPVFDG EGQLQPFFVT
VRNGDLKSIE LVAKGNEKVL RARLSDAKFF YEEDHKLTIE HALSKLENIV YHEELGSVAD
KVRRIRATSD LLSKQLLLDE QVTKEISRSA DICKFDLVSQ MVYEFPELQG IMGEDYALKA
GESKAVAKAI NEHYQPRFAG DLAPSEITGA IVSLADKIDT IVGCFSIGII PTGSQDPYAL
RRQAAGIVQI ILAHGLKLQL NELYDAALSV HEARGLKRDA AEIRKDLSDF FALRVKNVLS
EQGVRYDVID AVMASGFADL KSTIERATVV QALAASDDRS EFKLSVEQFN RVSNLGSKAD
GTTVDPALFA EQVETELYEK WLQQRPAFRS AIESGDMAKA VQSLSSLKPF IHTYFEKVMV
MAPDEAVRAN RLSTLAGIAE DIAIVADFSK LVW
//
