ID A0A1W9K0D8_9PROT Unreviewed; 760 AA.
AC A0A1W9K0D8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BVN33_00990 {ECO:0000313|EMBL:OQW77637.1};
OS Proteobacteria bacterium ST_bin13.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1978761 {ECO:0000313|EMBL:OQW77637.1, ECO:0000313|Proteomes:UP000192661};
RN [1] {ECO:0000313|EMBL:OQW77637.1, ECO:0000313|Proteomes:UP000192661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST_bin13 {ECO:0000313|EMBL:OQW77637.1};
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:OQW77637.1}.
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DR EMBL; MSXQ01000002; OQW77637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9K0D8; -.
DR Proteomes; UP000192661; 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 664..746
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
FT REGION 378..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 80027 MW; AFFF411A8C5D3DD6 CRC64;
MTDFLLELRS EEIPARMQAK AREDLARLFV TELAAAGLAA PAITTFSTPR RLTLIARSLP
LETAAVSEEI KGPKTAAPPQ ALDGFLRKTG LTRDQLVERD GVLFAVIDKP GRATADVLAE
AIPNIIRAFP WPKSMRWGDA SASTESLKWV RPLQGIVALL GGDVVPCAIA GITSGRETMG
HRFHSTGPIS IESAATYADQ LRDAHVIVDQ AERAQIIALG ATMAARKAGL ELIKDEGLLI
ENAGLTEWPV PLLGRFDDAF LSVPPEVIQL TARVNQKYFV CADADGNLAN AFICTANIDA
ADGGTKIVDG NRKVLAARLS DAKFFYDTDL KVKLADQATK LDRIVFHEKL GSVADKVDRV
AKLARWLVEE GIVKSSPLAG RGTSEAGGGG VPQPTASPSA TPLHHQPAAG GPPPRAGEDL
KEIATLAERA AKFCKADLVT LMVGEFPELQ GVMGGYYAAA QGEDPRVAAA IRDHYKPVGQ
GDDVPTDPVT VAVSLADKLD TLAKFFGINE GPTGSRDPFA LRRAAIGCLS LIIDNQLRLS
LASAISQALL PSAQGLDGWP PGIQLLSFLA DRLKVQQREA GVRHDLIDAV FALGGEDDLV
RLLARVHALQ AFIGTADGAN LLAGYKRAAN ILKKEGWAAS APAQAGALSS SDNPSNAGLR
PSPEHGAAAE NALPYTPEPA EVALIAALDV AEPAATAAVV AEDFEGAMAA LASLRAPIDA
FFETVIVNDP DPAKRTARLG LLARVRGAVH GVADFSKIEG
//
