ID A0A1I1D4J6_9ACTN Unreviewed; 465 AA.
AC A0A1I1D4J6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glycine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00253};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00253};
DE AltName: Full=Glycyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00253};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00253};
GN Name=glyQS {ECO:0000256|HAMAP-Rule:MF_00253};
GN ORFNames=SAMN04487968_10114 {ECO:0000313|EMBL:SFB69851.1};
OS Nocardioides terrae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=574651 {ECO:0000313|EMBL:SFB69851.1, ECO:0000313|Proteomes:UP000198832};
RN [1] {ECO:0000313|EMBL:SFB69851.1, ECO:0000313|Proteomes:UP000198832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7056 {ECO:0000313|EMBL:SFB69851.1,
RC ECO:0000313|Proteomes:UP000198832};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly).
CC {ECO:0000256|HAMAP-Rule:MF_00253}.
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|HAMAP-Rule:MF_00253};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00253}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00253}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00253}.
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DR EMBL; FOLB01000001; SFB69851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1D4J6; -.
DR STRING; 574651.SAMN04487968_10114; -.
DR OrthoDB; 9760853at2; -.
DR Proteomes; UP000198832; Unassembled WGS sequence.
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; cd00774; GlyRS-like_core; 1.
DR CDD; cd00858; GlyRS_anticodon; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR HAMAP; MF_00253_B; Gly_tRNA_synth_B; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR InterPro; IPR022961; Gly_tRNA_ligase_bac.
DR InterPro; IPR033731; GlyRS-like_core.
DR InterPro; IPR002315; tRNA-synt_gly.
DR NCBIfam; TIGR00389; glyS_dimeric; 1.
DR PANTHER; PTHR10745:SF0; GLYCINE--TRNA LIGASE; 1.
DR PANTHER; PTHR10745; GLYCYL-TRNA SYNTHETASE/DNA POLYMERASE SUBUNIT GAMMA-2; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00253};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00253}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00253};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00253};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00253};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00253}; Reference proteome {ECO:0000313|Proteomes:UP000198832}.
FT DOMAIN 10..369
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 199..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 209..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 214..218
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 286..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 326..330
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 330..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
SQ SEQUENCE 465 AA; 52783 MW; 39C4AF5F1BEF7689 CRC64;
MAKPPASTVD NVVSLAKRRG FVYPCGEIYG GTKSAWDYGP LGVELKDNIK RQWWRSMVTS
RDDVVGLDSS VILPRAVWEA SGHVATFTDP LVECLSCHHR FRADHLQEAF AEKKGIDNPD
DVALTEIACS NCGTRGQWTE PRNFSGLLKT YLGVIEDESG LHYLRPETAQ GIFVNFNNVV
TSQRVKPPFG IAQIGKSFRN EITPGNFIFR TREFEQMEME FFVKPGEDEE WHQYWIDTRT
AWYTDLGINP DNLRHYEHAQ EKLSHYSKRT VDIEYRFRFA GSEWGELEGI ANRTDFDLST
HSKHSGTDLS YFDQAANERY TPYVIEPAAG LSRSLMTFLV DAYTEDEAPN TKGGVDKRVV
LKLDPRLSPV KAAVLPLSRN EDLSPKARGL AAELRKSWNV DFDDAGAIGR RYRRQDEIGT
PFCITVDFDT LDDQAVTIRE RDTMAQERVS LDRVPAYLAE RLLGC
//
