ID A0A142LM65_9PROT Unreviewed; 715 AA.
AC A0A142LM65;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=AEM42_14630 {ECO:0000313|EMBL:AMS33311.1};
OS Betaproteobacteria bacterium UKL13-2.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1690485 {ECO:0000313|EMBL:AMS33311.1, ECO:0000313|Proteomes:UP000075227};
RN [1] {ECO:0000313|Proteomes:UP000075227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Driscoll C.B.;
RL Submitted (JUL-2015) 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|ARBA:ARBA00011209, 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}.
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DR EMBL; CP012157; AMS33311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142LM65; -.
DR STRING; 1690485.AEM42_14630; -.
DR KEGG; beb:AEM42_14630; -.
DR PATRIC; fig|1690485.4.peg.3327; -.
DR Proteomes; UP000075227; 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 {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:UP000075227}.
FT DOMAIN 607..702
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 715 AA; 78523 MW; 2CEDAC9D7716C57F CRC64;
MSSDSKKELL LVELFTEELP PKVLKKLGDA FASGIHAGLI SRGLVAADAK VEMFATPRRL
AVRIADVAGI ADDRAELKKL MPVKVAFDAA GNPTPALQKR LEKESATLAN TVRKVDGADE
LVYLDVTIKG AWLRDALQAA LLDSMAKLPI PKMMTYQLAN GLDSVQFVRP AHGLVAMHGA
EVVAVETLGL HAGNVIHGHR FQGEKTMTLA HASEYESCLE KDGGVIASFK KRRHEIERLL
IAHAEQCGDT LGERSEYLAL LDEVTALVEL PTVYVGKFER EFLEVPAECL TLTMKLNQKY
FPLHLSEGGL SSRFLIVSNM RLDDARNIVE GNQRVVRPRL ADARFFFNTD KKTKLVDRLP
KLASVVYHNK LGSQGERVER VRAIAKAICE LTNQDAVFQA SVDQAAQLAK ADLVTDMVGE
FPELQGTMGK YYALNEGIDA VVAEAIEDHY KPKFAGDTLP RSQVGVIVAL ADKLETLAGL
FAMGQQPTGD KDPFALRRHA LGVLRLIMEE RLPLKLENLL KLGFDTIPPE LVSTDLEEGD
ALISFQQIQL ERFLFERLNG LLRDQAFTAQ EVDAVLSLKP DRLEKVKDRL NAVRTFAALP
EAPSLAAANK RIGNILKKAD GVKEAYDKSL TTEVAETALA VAMESVVPHA KAQFDRGDYT
ASLTSLATLR EPVDTFFEKV MVNADDPAIR ANRLGLLATL HREMNRVADL SKLAA
//
