ID A0A1W9GUL6_9PROT Unreviewed; 816 AA.
AC A0A1W9GUL6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
GN Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN ORFNames=A4S12_02785 {ECO:0000313|EMBL:OQW38823.1};
OS Proteobacteria bacterium SG_bin5.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1827382 {ECO:0000313|EMBL:OQW38823.1, ECO:0000313|Proteomes:UP000192868};
RN [1] {ECO:0000313|EMBL:OQW38823.1, ECO:0000313|Proteomes:UP000192868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG_bin5 {ECO:0000313|EMBL:OQW38823.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
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:OQW38823.1}.
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DR EMBL; LWDI01000104; OQW38823.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9GUL6; -.
DR Proteomes; UP000192868; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR NCBIfam; TIGR00211; glyS; 1.
DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 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_00255};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00255};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00255}.
FT DOMAIN 734..807
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
FT REGION 384..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..697
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 86978 MW; 8D7EABF88FE416F1 CRC64;
MTDFLLELRS EEIPARMQAR AREDLAKLFV AELAKAGLAA GEIVTYATPR RLALIARRLP
EATEAVSEEI KGPRASAPPQ ALEGFLRKTG LAREALVERD GILFAVIERP GRATADLLAE
AVPAIVRAFP WPKSMRWGAA SLSTESLRWV RPLQGIVALF GDEVVPCEVA GIASGRETYG
HRFMAPGAIA IESAASYVEQ LRAAHVIVDQ DERAAIIRDR AAALAAEAGL ALVADEGLVA
ENAGLTEWPV PLLGRFDEAF LSVPPEVIQL TARVNQKYFV CQDGGGKLAN AFICVANIQA
ADGGAKIVEG NRKVLAARLS DARFFYEQDL RVPLDDQAAK LDRIVFHEKL GTVADKVRRV
AKLARWLVEE GIIKPLPFRG GVGGGGGATN AAPGSESPHP NPSPEGEGLS ASELAALAER
AALLCKADLV TLMVGEFPEL QGVMGGYYAA AQGEHPAVAE AIRDHYKPVG QGDDVPTAPV
TVAVSLADKL DTIVEFFSVD EKPTGSRDPF ALRRSALGVL TILIENGVRL NFGAVFWNGV
SDRIGKGTLF HSEGGDLRPF SRNEVERFRS ERLNALSRDV VSFLTDRLKV QQREAGVRHD
LIDAVFALGG EDDLVRLLAR VRALQGFVTT EDGANLLAGY KRAANILKKE APESPAHAPA
DPAGMAERLG GGTSGPGAAF GPGHDILPPP PPGRDIPQTG EEDPLVEVDD PEFAPIVAEL
ARGERHKALG YTPEPAEEAL IAALDAAEPA ARTAIAHEDF EGAMAALAAL RAPIDAFFED
VTVNDPEPAK RAARLALLAR VRDAVHQVAD FSKIEG
//
