ID A0A2G1WNG3_9EURY Unreviewed; 594 AA.
AC A0A2G1WNG3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=glycine--tRNA ligase {ECO:0000256|ARBA:ARBA00012829};
DE EC=6.1.1.14 {ECO:0000256|ARBA:ARBA00012829};
GN ORFNames=DJ69_00255 {ECO:0000313|EMBL:PHQ40540.1};
OS Halorubrum persicum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1383844 {ECO:0000313|EMBL:PHQ40540.1, ECO:0000313|Proteomes:UP000222824};
RN [1] {ECO:0000313|EMBL:PHQ40540.1, ECO:0000313|Proteomes:UP000222824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C49 {ECO:0000313|EMBL:PHQ40540.1,
RC ECO:0000313|Proteomes:UP000222824};
RX PubMed=24782836; DOI=10.3389/fmicb.2014.00140;
RA Fullmer M.S., Soucy S.M., Swithers K.S., Makkay A.M., Wheeler R.,
RA Ventosa A., Gogarten J.P., Papke R.T.;
RT "Population and genomic analysis of the genus Halorubrum.";
RL Front. Microbiol. 5:140-140(2014).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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:PHQ40540.1}.
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DR EMBL; NHOA01000003; PHQ40540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G1WNG3; -.
DR OrthoDB; 6113at2157; -.
DR Proteomes; UP000222824; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00774; GlyRS-like_core; 1.
DR Gene3D; 3.30.40.230; -; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:PHQ40540.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 4..470
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 594 AA; 65198 MW; 9E16FAB9B31BC2EE CRC64;
MASEAIVELA KRRGFFFGSN GAYGGTAGFY TFGPQGAALK KNVEDAWRDR FTIREGNREI
EAPTIMPEPV FEASGHLDTF DDMLVECPEC GESHRADHLV EAVTEIEDAE ALPGSEVEEL
IADNDIACPS CGTALAGVTV EDFNLMFATD IGPGDAQPGY LRPETAQGIF VEFPRLKEYA
RGNLPFGITQ IGPAYRNEIS PRGGLLRLRE FTQAELEQFI DPEEDEPPLD RVRDVSVRLY
PATEQQAEDG EYVETTVGEA VDEGTIGSPW VGYYLGVAKR WYDRIGVDLD RFRFRQHLAG
ERAHYASDCW DAESEVDGDW IEIAGFSYRA DYDLSKHDAH GDDAFTVFKR YDEPKTVERA
TVDPDMSVLG PEFGGDAAAV AEALETLAER DPDAFDGETV SVEAAGETHE VDADVANFSV
ETVTENGEHL TPHVVEPSFG VGRTVQTLLA HAYSEDEVDG EERTYLSLEP EVAPQDAAVF
PLVTNDDRLT ELADRVATDL REAGLAVAYD DSGSIGRRYR RQDEIGTPFC VTIDRDGIEG
DGPETVTVRE RDSAAQVRVP AEELAEELAA LRAGGEFDAL VDRYETVATD VETN
//
