SYG_STRCO
ID SYG_STRCO Reviewed; 460 AA.
AC Q9L2H9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glycine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00253};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00253};
DE AltName: Full=Glycyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00253};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00253};
GN Name=glyQS {ECO:0000255|HAMAP-Rule:MF_00253}; Synonyms=glyS;
GN OrderedLocusNames=SCO2504; ORFNames=SCC121.07c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly).
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00253};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00253}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00253}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00253}.
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DR EMBL; AL939112; CAB69725.1; -; Genomic_DNA.
DR RefSeq; NP_626744.1; NC_003888.3.
DR RefSeq; WP_003976298.1; NZ_VNID01000001.1.
DR AlphaFoldDB; Q9L2H9; -.
DR SMR; Q9L2H9; -.
DR STRING; 100226.SCO2504; -.
DR PRIDE; Q9L2H9; -.
DR GeneID; 1097938; -.
DR KEGG; sco:SCO2504; -.
DR PATRIC; fig|100226.15.peg.2549; -.
DR eggNOG; COG0423; Bacteria.
DR HOGENOM; CLU_015515_2_1_11; -.
DR InParanoid; Q9L2H9; -.
DR OMA; EPSYGID; -.
DR PhylomeDB; Q9L2H9; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00774; GlyRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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 PANTHER; PTHR10745; PTHR10745; 3.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00389; glyS_dimeric; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..460
FT /note="Glycine--tRNA ligase"
FT /id="PRO_0000072981"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 194..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 204..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 209..213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 281..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 321..325
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 325..328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
SQ SEQUENCE 460 AA; 52440 MW; 259ED0401C781ED3 CRC64;
MAADKIDTIV SLSKRRGFVF PCSEIYGGQR AAWDYGPLGV ELKENLKRQW WRYMVTSRED
VVGLDSSVIL APEVWVASGH VATFTDPLTE CTSCHKRFRA DHLEEAYEEK KGHAPENGLA
DLNCPNCGNK GTFTEPKQFS GLLSTHLGPT QDSGSVAYLR PETAQGIFTN FAQVQTTSRR
KPPFGIAQMG KSFRNEITPG NFIFRTREFE QMEMEFFVKP GEDEKWQEYW MEQRWNWYTG
LGLREENMRW YEHPAEKLSH YSKRTADIEY RFSFGGSEWG ELEGVANRTD YDLSSHAKAS
GQDLSYYDQE AQERWTPYVI EPAAGVGRAM LAFLLDAYIE DEAPNAKGKL EKRTVLRLDP
RLSPVKVAVL PLSRNPELSP KAKGLAQALR QNWNIEFDDA GAIGRRYRRQ DEIGTPFCVT
VDFDTLDDNA VTVRERDTMK QERVSLDQIE GYLASRLVGC
