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Database: UniProt
Entry: A0A0G3ILY8_9MYCO
LinkDB: A0A0G3ILY8_9MYCO
Original site: A0A0G3ILY8_9MYCO 
ID   A0A0G3ILY8_9MYCO        Unreviewed;       466 AA.
AC   A0A0G3ILY8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=AB431_19805 {ECO:0000313|EMBL:AKK28543.1};
OS   Mycobacterium sp. EPa45.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK28543.1, ECO:0000313|Proteomes:UP000035237};
RN   [1] {ECO:0000313|Proteomes:UP000035237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPa45 {ECO:0000313|Proteomes:UP000035237};
RA   Kato H., Ogawa N., Ohtsubo Y., Ohshima K., Toyoda A., Yamazoe A., Mori H.,
RA   Maruyama F., Nagata Y., Hattori M., Fujiyama A., Kurokawa K., Tsuda M.;
RT   "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT   Strain EPa45, Isolated from a Phenanthrene-Degrading Consortium.";
RL   Genome Announc.0:0-0(2015).
RN   [2] {ECO:0000313|EMBL:AKK28543.1, ECO:0000313|Proteomes:UP000035237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPa45 {ECO:0000313|EMBL:AKK28543.1,
RC   ECO:0000313|Proteomes:UP000035237};
RX   PubMed=26184940;
RA   Kato H., Ogawa N., Ohtsubo Y., Oshima K., Toyoda A., Mori H., Nagata Y.,
RA   Kurokawa K., Hattori M., Fujiyama A., Tsuda M.;
RT   "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT   Strain EPa45 (NBRC 110737), Isolated from a Phenanthrene-Degrading
RT   Consortium.";
RL   Genome Announc. 3:e00782-15(2015).
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; CP011773; AKK28543.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G3ILY8; -.
DR   STRING; 1545728.AB431_19805; -.
DR   KEGG; mye:AB431_19805; -.
DR   PATRIC; fig|1545728.4.peg.4030; -.
DR   OrthoDB; 9760853at2; -.
DR   Proteomes; UP000035237; 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}.
FT   DOMAIN          6..370
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         200..202
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         210..215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         215..219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         287..288
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         327..331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         331..334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
SQ   SEQUENCE   466 AA;  52866 MW;  5E071377752181CD CRC64;
     MASVIDSVVN LAKRRGLVYP AGEIYGGTKS AWDYGPLGVE LKENIKRQWW RSVVTGRDDV
     VGLDSSIILP REVWVASGHV EVFHDPLIEC LNCHKRHRQD HLQEAYAEKK AAKEKTEVDP
     ESVAMTEIVC PDCGTKGQWT EPREFNMMLK TYLGPIESEE GLHYLRPETA QGIFVNFANV
     VTTSRKKPPF GIGQIGKSFR NEITPGNFIF RTREFEQMEM EFFVEPATAP EWHQYWIDTR
     LQWYIDLGIN RDNLRLFVHP QEKLSHYSAG TTDIEYKFGF GGNPWGELEG IANRTDFDLK
     THSQHSGTDL SFYDQAADTR YIPYVIEPAA GLTRSFMAFL VDAYAEDEAP NAKGGVDKRT
     VLRLDPRLAP VKAAVLPLSR HADLSPKAKD LAAELRKNWN IEFDDAGAIG RRYRRQDEIG
     TPYCVTVDFD TLEDHAVTVR ERDQMTQERI SIDSVVDYLA TKLAGG
//
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