ID A0A208XNR9_9BURK Unreviewed; 710 AA.
AC A0A208XNR9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=CDO44_17590 {ECO:0000313|EMBL:OVZ57571.1};
OS Pigmentiphaga sp. NML080357.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pigmentiphaga.
OX NCBI_TaxID=2008675 {ECO:0000313|EMBL:OVZ57571.1, ECO:0000313|Proteomes:UP000196551};
RN [1] {ECO:0000313|EMBL:OVZ57571.1, ECO:0000313|Proteomes:UP000196551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML080357 {ECO:0000313|EMBL:OVZ57571.1,
RC ECO:0000313|Proteomes:UP000196551};
RA Bernier A.-M., Bernard K.;
RT "Pigmentiphaga species Genome sequencing and assembly.";
RL Submitted (MAY-2017) 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}.
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:OVZ57571.1}.
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DR EMBL; NINW01000038; OVZ57571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A208XNR9; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000196551; 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 601..701
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 710 AA; 75810 MW; BFBEB06C4364E0F7 CRC64;
MPAAQPLLLE LFTEELPPKA LNRLGQAFAD GIAAGLQGRG LVAEGNTVTA YATPRRLAVR
LSAVLPQAAD TEFSEKLMPV SVGLTADGQA TPALLKKLAA KGLETIDISG LARESDGKNE
QLVYHGIAKG AALAAALQTV LEDTLGKLPI PKVMSYQLAD GATTVRFVRP AHGLVALHGD
AVVDVTALGL RAGRVTRGHR FQSEGPIELA SADVYEDRLH DQGRVIASFA QRRAAIERQL
RDQASRLHAS LGDEADVASL LDEVCALVEY PTVYVGEFES EFLAVPQECL ILTMRLNQKY
FPLFDAATGK LTHRFLIVSN MALANPSNIV EGNQRVVRPR LADARFFFET DKKVPLAGRV
EQLGTVVYHN KLGTQLERSQ RVRALARWVA EAIGADPGRA DRAALLAKAD LVTGMVGEFP
ELQGIMGAYY AAADGETPDV VEAIRQQYRI RLEQPVTDDT ATMAALFLAE RAETLLGIWS
IGLVPTGDKD PYGLRRAALG LISAFEQLDA GGRLPADGSG LTLDGLLARA ASTFATPPTA
AQIDEVRAFI FERYRNQLAG QFDRAAVDAV VAVAPPLAQV PARVRAVVAF SALPEAAALA
AANKRIGNLL KKVEGEPGPV NEALLAEPAE QALAQTLRTL RPQAEGKFAL GDFAGALTVL
SQARGPVDAF FADVMVMAED PATRANRLAL LAELHRVMNH VADLSRLATA
//
