GenomeNet

Database: UniProt
Entry: A0A023X149_9ACTN
LinkDB: A0A023X149_9ACTN
Original site: A0A023X149_9ACTN 
ID   A0A023X149_9ACTN        Unreviewed;       461 AA.
AC   A0A023X149;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   13-SEP-2023, entry version 46.
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=RradSPS_0648 {ECO:0000313|EMBL:AHY45931.1};
OS   Rubrobacter radiotolerans.
OC   Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=42256 {ECO:0000313|EMBL:AHY45931.1, ECO:0000313|Proteomes:UP000025229};
RN   [1] {ECO:0000313|EMBL:AHY45931.1, ECO:0000313|Proteomes:UP000025229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSPS-4 {ECO:0000313|EMBL:AHY45931.1,
RC   ECO:0000313|Proteomes:UP000025229};
RA   Egas C.C., Barroso C.C., Froufe H.J.C., Pacheco J.J., Albuquerque L.L.,
RA   da Costa M.M.S.;
RT   "Complete genome sequence of the Radio-Resistant Rubrobacter radiotolerans
RT   RSPS-4.";
RL   Submitted (MAR-2014) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP007514; AHY45931.1; -; Genomic_DNA.
DR   RefSeq; WP_038680681.1; NZ_CP007514.1.
DR   AlphaFoldDB; A0A023X149; -.
DR   STRING; 42256.RradSPS_0648; -.
DR   KEGG; rrd:RradSPS_0648; -.
DR   PATRIC; fig|42256.3.peg.659; -.
DR   eggNOG; COG0423; Bacteria.
DR   HOGENOM; CLU_015515_2_1_11; -.
DR   OrthoDB; 9760853at2; -.
DR   Proteomes; UP000025229; Chromosome.
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:SF8; DNA POLYMERASE SUBUNIT GAMMA-2, MITOCHONDRIAL; 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:UP000025229}.
FT   DOMAIN          8..366
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         203..205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         213..218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         218..222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         288..289
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         328..332
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         332..335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
SQ   SEQUENCE   461 AA;  53490 MW;  3F7A77331B6C2790 CRC64;
     MSETVTMEKI VSFCKRRGFI FQSSEIYGGI RSAYDYGPLG VEMKRNVKDE WWRTMVHTRD
     DVVGVDAAII MHPRVWEASG HVGTFNDMLV ESRTSGRRYR ADHLIEAATG RDDIEGLSAE
     EMTEIIQTDE RVKDPLDGGR DFAPVRPFNL MFETYTGPVK SPENIAYLRP ETAQGIFTNF
     KNVLDTSRVK VPFGIAQQGK SFRNEITPGN FIFRTREFEQ MEMEFFVEPG TDEGWHEYWL
     EERWRWYTDL GLNPDNLRRY EHPKEKLSHY SKRTVDIEYD FPFSGWSELE GIANRTDYDL
     KRHAEFSGQK LEYRDQQANR SYVPYVIEPA VGVDRITLAF LVDAYREEEV EGETRTVLKL
     HPRLAPVKAA VFPLTKKEPV STVAKKLYDD LKGDYRIAYD DGGSIGRRYR RQDEAGTPFC
     VTVDFDTLED KQVTIRDRDT MQQERIPIEA VRDRLKALIS G
//
DBGET integrated database retrieval system