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Database: UniProt
Entry: A0A0M2NNA1_9FIRM
LinkDB: A0A0M2NNA1_9FIRM
Original site: A0A0M2NNA1_9FIRM 
ID   A0A0M2NNA1_9FIRM        Unreviewed;       460 AA.
AC   A0A0M2NNA1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=CHK_0852 {ECO:0000313|EMBL:KKI51685.1};
OS   Christensenella hongkongensis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Christensenellaceae;
OC   Christensenella.
OX   NCBI_TaxID=270498 {ECO:0000313|EMBL:KKI51685.1, ECO:0000313|Proteomes:UP000034076};
RN   [1] {ECO:0000313|EMBL:KKI51685.1, ECO:0000313|Proteomes:UP000034076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKU16 {ECO:0000313|EMBL:KKI51685.1,
RC   ECO:0000313|Proteomes:UP000034076};
RA   Lau S.K., Teng J.L., Huang Y., Curreem S.O., Tsui S.K., Woo P.C.;
RT   "Draft genome sequence of bacteremic isolate Catabacter hongkongensis type
RT   strain HKU16T.";
RL   Submitted (APR-2015) 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:KKI51685.1}.
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DR   EMBL; LAYJ01000068; KKI51685.1; -; Genomic_DNA.
DR   RefSeq; WP_046442772.1; NZ_SMCZ01000006.1.
DR   AlphaFoldDB; A0A0M2NNA1; -.
DR   STRING; 270498.CHK_0852; -.
DR   PATRIC; fig|270498.16.peg.451; -.
DR   OrthoDB; 9760853at2; -.
DR   Proteomes; UP000034076; 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:0016740; F:transferase activity; IEA:UniProt.
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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000034076}.
FT   DOMAIN          152..367
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         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         204..206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         214..219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT   BINDING         219..223
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   460 AA;  53040 MW;  1BBCFC7B369CB96A CRC64;
     MEKTMEKIVA LAKGRGFVFP GSEIYGGLAN SWDYGPLGVE FKNNVKRAWW QKFVQECPYN
     VGLDSAILMN PETWVASGHV GGFNDPLMDC KSCKERFRAD KLIEDYAAEN DLDIGSVEAM
     SKEEMEAFIA ENIVCPSCGK KDFTPIRQFN LMFKTFQGVN EDTAAQIYLR PETAQGIFVN
     FKNVLRTTRR KMPMGIGQVG KSFRNEITPG NFIFRIREFE QMELEFFCDP KEEFEWFKYW
     KDYCHNWLLS LGIDDENLKL RDHAPEELSH YSNATTDIEY RFPFGWGELW GIADRTDFDL
     KAHMAHSGES LEYLDPVTNE KYVPYCIEPS LGADRVALAF LCEAYDEETL ENGDTRIVMH
     LHPALAPFKA AVLPLQKKLS ETSDKLFADL SRHFNVDYDL AGSIGKRYRR EDEIGTPYCI
     TVDFETLDDK CVTVRDRDTM QQERIAMDQV QKFLEDKLVF
//
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