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Database: UniProt
Entry: A0A136LDN3_9BACT
LinkDB: A0A136LDN3_9BACT
Original site: A0A136LDN3_9BACT 
ID   A0A136LDN3_9BACT        Unreviewed;       334 AA.
AC   A0A136LDN3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-JUN-2023, entry version 20.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000256|HAMAP-Rule:MF_00254};
GN   ORFNames=UZ18_ATM001000602 {ECO:0000313|EMBL:KXK19687.1};
OS   Armatimonadetes bacterium OLB18.
OC   Bacteria; Armatimonadota.
OX   NCBI_TaxID=1617424 {ECO:0000313|EMBL:KXK19687.1, ECO:0000313|Proteomes:UP000070351};
RN   [1] {ECO:0000313|EMBL:KXK19687.1, ECO:0000313|Proteomes:UP000070351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB18 {ECO:0000313|EMBL:KXK19687.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Improved understanding of the partial-nitritation anammox process through
RT   23 genomes representing the majority of the microbial community.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000201,
CC         ECO:0000256|HAMAP-Rule:MF_00254};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00254}.
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:KXK19687.1}.
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DR   EMBL; JZQX01000086; KXK19687.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136LDN3; -.
DR   STRING; 1617424.UZ18_ATM001000602; -.
DR   PATRIC; fig|1617424.3.peg.646; -.
DR   Proteomes; UP000070351; 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   HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR   PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00254};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00254}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00254};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00254};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00254}.
SQ   SEQUENCE   334 AA;  37845 MW;  2B919BD7F1D66E7C CRC64;
     MTFQELVFRL NKYWAEQGCA ILQPYDVEMG AGTMHPATSL RALGPEPWNV AYVQPSRRPA
     DGRYTRNPMR SQRYYQYQVM LKPSPEDVVD VYLGSLNALG FDVTKNDVRL VEDDWESPSV
     GASGVGWEVW LDGTEITQFT FFQQMGGIEC NPVCAEITYG PERLCLMLSK GHSFWEGLMW
     NDSLSYFQTD YQLEMQHNVY NFEVADVEML FRLFEMYESE SKRVIETPVY WESEKRVLTT
     AAADDEDPLA KRKAGLALVY PAYDLALKCS HAFNLLDARG AISPTARADY ITRIRAGSGP
     VALDTSSSSK SPQRRPRFSG LAICLRLAFV HDPS
//
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