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Database: UniProt
Entry: A0A1G2FXF9_9BACT
LinkDB: A0A1G2FXF9_9BACT
Original site: A0A1G2FXF9_9BACT 
ID   A0A1G2FXF9_9BACT        Unreviewed;       430 AA.
AC   A0A1G2FXF9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=glycine--tRNA ligase {ECO:0000256|ARBA:ARBA00012829};
DE            EC=6.1.1.14 {ECO:0000256|ARBA:ARBA00012829};
GN   ORFNames=A2W41_03435 {ECO:0000313|EMBL:OGZ42412.1};
OS   Candidatus Ryanbacteria bacterium RIFCSPHIGHO2_01_45_13.
OC   Bacteria; Candidatus Ryanbacteria.
OX   NCBI_TaxID=1802112 {ECO:0000313|EMBL:OGZ42412.1, ECO:0000313|Proteomes:UP000176700};
RN   [1] {ECO:0000313|EMBL:OGZ42412.1, ECO:0000313|Proteomes:UP000176700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGZ42412.1}.
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DR   EMBL; MHNI01000018; OGZ42412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2FXF9; -.
DR   Proteomes; UP000176700; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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   CDD; cd00858; GlyRS_anticodon; 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:OGZ42412.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          5..331
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   430 AA;  50136 MW;  44F33DAF7E194148 CRC64;
     MVNLDVIVSL AKRRGFLWRS SDIYGGLSGA WDFGPMGVEL ARNIKQLWWK KFIQERDDMY
     GIDASILMNA RTWEASGHIE GFHDPLVECK KCKRRFRADQ AQDQCPECGG ALTKERQFNM
     MFETRVGAVE DSASITYLRP ETAQGMFVNF KNILDAFHPL IPFGIGQTGK AFRNEITPKD
     FIFRIREFEQ MEIEYFVREK EWETYFNHWK SEMWAWIENI GLARSRVHEL EVPSNERAHY
     SRRTIDFEYD FPFGRQELYG LAYRADFDLR QHSKASGVEL QYFNEGSGER FYPHVIEPTF
     GVERTVLALL CDAYKEDVLG GDARVYLALK PHLAPVQAAV FPLLRNNKSL VSKARAVYKD
     IKKAVPQMMW DDNGNIGKRY RRQDEIGTPW CITIDHQTLD DDTVTIRDRD SGEQKRVHIH
     EVSLFIKEEK
//
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