ID A0A327VJV7_9ACTN Unreviewed; 460 AA.
AC A0A327VJV7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=K377_07026 {ECO:0000313|EMBL:RAJ73597.1};
OS Streptomyces sp. PsTaAH-137.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1305830 {ECO:0000313|EMBL:RAJ73597.1, ECO:0000313|Proteomes:UP000249376};
RN [1] {ECO:0000313|EMBL:RAJ73597.1, ECO:0000313|Proteomes:UP000249376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PsTaAH-137 {ECO:0000313|EMBL:RAJ73597.1,
RC ECO:0000313|Proteomes:UP000249376};
RA Currie C.;
RT "Biomass-degrading enzyme discovery via genome sequencing of insect-
RT associated Streptomyces.";
RL Submitted (JUN-2018) 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}.
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:RAJ73597.1}.
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DR EMBL; QLLY01000022; RAJ73597.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327VJV7; -.
DR OrthoDB; 9760853at2; -.
DR Proteomes; UP000249376; 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}.
FT DOMAIN 4..360
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 194..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 204..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 209..213
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 281..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 321..325
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 325..328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
SQ SEQUENCE 460 AA; 52629 MW; 577925E02B3F49B3 CRC64;
MAADKIETIV SLSKRRGFVY PCSEIYGGQR AAWDYGPLGV ELKENLKRQW WRYMVTARED
VVGIDSSVIL ATEVWQASGH VATFTDPLTE CTSCHKRFRA DHLEEAYEEK KGRAPENGLA
DLTCPNCGNK GTFTEPKQFS GLLSTHLGPT QDSGSVAYLR PETAQGIFTN FAQVQTTSRR
KPPFGIAQMG KSFRNEITPG NFIFRTREFE QMEMEFFVKP GEDEKWQEYW MEQRWNWYTG
LGLREENMRW FEHPKEKLSH YSKRTADIEY RFRFGGSEWG ELEGVANRTD YDLSAHSKAS
GQDLSYFDQE KGERYTPYVI EPAAGVGRTM LAFMLDSYFE DEAPNAKGKM EKRTVMRFDP
RIAPVKVAVL PLSRNPELSP KAKGLAAALR QNWNIDFDDA GAIGRRYRRQ DEIGTPFCVT
VDFDTLEDNA VTVRERDTMK QERVSLDQIE GYLAARLVGC
//
