ID A0A370AZJ8_9SPIO Unreviewed; 461 AA.
AC A0A370AZJ8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=DV872_02805 {ECO:0000313|EMBL:RDG33852.1};
OS Oceanispirochaeta sp. M1.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Oceanispirochaeta.
OX NCBI_TaxID=2283433 {ECO:0000313|EMBL:RDG33852.1, ECO:0000313|Proteomes:UP000253869};
RN [1] {ECO:0000313|EMBL:RDG33852.1, ECO:0000313|Proteomes:UP000253869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:RDG33852.1,
RC ECO:0000313|Proteomes:UP000253869};
RA Yadav S., Villanueva L., Damste J.S.S.;
RT "Draft genome sequence of Oceanispirochaeta sp. strain M1.";
RL Submitted (JUL-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:RDG33852.1}.
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DR EMBL; QQPQ01000003; RDG33852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370AZJ8; -.
DR OrthoDB; 9760853at2; -.
DR Proteomes; UP000253869; 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:UP000253869}.
FT DOMAIN 19..369
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 193..195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 203..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 208..212
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 318..322
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 322..325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
SQ SEQUENCE 461 AA; 53142 MW; 01D91EF1210DA8D2 CRC64;
MAKEKKANQI SNKFGASMEK IVSLAKRRGF VYPSSEIYGG LSATWDYGPL GVELKKNIQE
IWWREMTRLQ DNIVGLDAAI MMHPRTWEAS GHVENFSDPL VDCKQCKTRF REDKLTPEVI
ASKKCPECGG ELTEPRQFNL MFSTHLGPVA DSGSIVYLRP ETAQGIFVNF RNVVDTSRVT
VPFGIAQVGK AFRNEITTKN FIFRTCEFEQ MEMQFFVKPG TDDEWFEYWK EQRMKYYTEQ
LGVLPENLHF HQHGPDELAH YAKDAYDVEY QYPFGWEEQE GVHNRTDFDL GRHAEFSGKK
INYLDPHTNE RYVPYVIETS AGLTRSVLVC LMDAYHEQTI GTDKNGNPDV RTVLHLHPNV
APVKAAVLPL VKKDGLADLA KEIQKELSED FNAFYDQSGA IGRRYRRQDE IGTPFCITVD
YDSKENNDVT IRFRDSMEQI RVPREGLAAR LKEEIKKYKR V
//
