ID A0A1H4FWX0_9BURK Unreviewed; 717 AA.
AC A0A1H4FWX0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=SAMN05444680_105259 {ECO:0000313|EMBL:SEB01839.1};
OS Variovorax sp. YR216.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882828 {ECO:0000313|EMBL:SEB01839.1, ECO:0000313|Proteomes:UP000199122};
RN [1] {ECO:0000313|Proteomes:UP000199122}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR216 {ECO:0000313|Proteomes:UP000199122};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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_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}.
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DR EMBL; FNRO01000005; SEB01839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4FWX0; -.
DR STRING; 1882828.SAMN05444680_105259; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000199122; 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 609..702
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 717 AA; 77061 MW; 3D254DA965725992 CRC64;
MTTKNNLLVE LFVEELPPKA LRKLGEAFAT VLRDQLVAAG LADAGSVLTP YASPRRLAAH
LTNVLAQAAD KAVSQKLMPV SVGLDASGNP TPALLKRLGA LGADASVVPE LRRAMDGKAE
ALFYESTAKG ATLAEGLQKA LAEAIAKLPI PKVMSYQLES GCELPGWSSV SFVRPAHGLV
ALHGDTVVPV EALGLQAGRE THGHRFEASV DPVSLRDANG YDQQLQDEGA VIPGFEARRA
EIARQLAEAA IKVGGNTQPI NDDALLDEVT ALVERPNVLI CEFEREFLDV PQECLILTMK
ANQKYFPLLD AHGRLTNKFL VVSNINPADA SAVIGGNERV VRPRLADAKF FFDQDRKKSL
ASRVESLAKV VYHNKLGTQG ERVERVMRIA HAIGEKIGTP IGDAHLAPRA VQAAQLAKAD
LVTDMVGEFP ELQGIMGRYY ALHDGLDHTV ADAIEDHYKP RFAGDELPRS NVGIVVALAD
KLETLVGMFG IGNLPTGDRD PFALRRHALG VIRMLIERNL SLDLRTMLSD AFAAFGAHKG
GEIALTDPTD ALEAFIYDRL AGSLREQGAS AQEVEAVLSP RPQRLAEVPK LLAAVRAFAA
LPEAPALAAA NKRIGNILKK SPEADAHVSE LLLKEPAEKA LHAAMQQVVP VANGQFEAGD
YTASLQTLAA LRDPVDAFFD DVMVNAEQSD LRLNRLGLLM ILHGAMNRVA QLERLAA
//