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Database: UniProt
Entry: A0A1H4FWX0_9BURK
LinkDB: A0A1H4FWX0_9BURK
Original site: A0A1H4FWX0_9BURK 
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
//
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