ID A0A261UR82_9BORD Unreviewed; 712 AA.
AC A0A261UR82;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=CAL28_06925 {ECO:0000313|EMBL:OZI64404.1};
OS Bordetella genomosp. 11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1416808 {ECO:0000313|EMBL:OZI64404.1, ECO:0000313|Proteomes:UP000215767};
RN [1] {ECO:0000313|EMBL:OZI64404.1, ECO:0000313|Proteomes:UP000215767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU8856 {ECO:0000313|EMBL:OZI64404.1,
RC ECO:0000313|Proteomes:UP000215767};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
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:OZI64404.1}.
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DR EMBL; NEVS01000002; OZI64404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261UR82; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000215767; 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 605..699
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 712 AA; 76275 MW; F6F46E27E30E3C9C CRC64;
MSDVRPLLVE LLTEELPPKA LRKLGDAFAE GIRQGLAQRG LLAADCRMQP YATPRRLAVH
LSAVLAQAPD QEYAEKLMPV KVGLDAEGRP TPALLKKLAA KGLDAVDAAT LARESDGKQD
YLVARGTAPG ARLADGLQHA LDAAIAGLPI PKVMGYQLAD GVTTVKFVRP AHGLVALFGP
DVVDIAALGL SAGRDTLGHR FMSEGPIALR DADAYAGQLA ETGRVIAGFD ARRDEISRQL
DVHASRLGAT LGNDPEVPAL LDEVTALVEH PTVYVGEFEP RFLQVPQECL ILTMRLNQKY
FPLFAPDTGK LTHRFLIVSN MQVADPVNIV EGNQRVVRPR LADAQFFFET DRKTPLAARV
DQLGSIVYHN KLGTQLQRVE RVRAVARGVA QALGVAPQAA DRAALLAKAD LGTLMVGEFP
ELQGVMGAYY AEADGEAPDV VRALREQYRN RLDAPVDRDG LTMATLFIAE RAETLVGIWS
IGLAPTGERD PYGLRRAALG LISAFEQLAA GGWLKPSENG PLSVQGVLRL AADSFGPDQK
IAAEVLGEVG DFIYERYRNQ LAAEFDRNAV DAVIALTPPL HQVAARVRAV TAFGALPEAA
SLAAANKRVG NLLKKTEGDI GAVDAARLVE PAELALAQAI ERLSPRAQSQ FDEGDFAGSL
STLAQAREPV DAFFADVMVM ADDPAVRANR LALLGELHGL MNKVADISRL AQ
//
