ID B6B2U7_9RHOB Unreviewed; 685 AA.
AC B6B2U7;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 ECO:0000313|EMBL:EDZ44357.1};
GN ORFNames=RB2083_3872 {ECO:0000313|EMBL:EDZ44357.1};
OS Rhodobacteraceae bacterium HTCC2083.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ44357.1, ECO:0000313|Proteomes:UP000005746};
RN [1] {ECO:0000313|Proteomes:UP000005746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2083 {ECO:0000313|Proteomes:UP000005746};
RX PubMed=21036993; DOI=10.1128/JB.01268-10;
RA Kang I., Vergin K.L., Oh H.M., Choi A., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of strain HTCC2083, a novel member of the marine clade
RT Roseobacter.";
RL J. Bacteriol. 193:319-320(2011).
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; DS995276; EDZ44357.1; -; Genomic_DNA.
DR AlphaFoldDB; B6B2U7; -.
DR STRING; 314270.RB2083_3872; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_1_5; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000005746; 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}; Reference proteome {ECO:0000313|Proteomes:UP000005746}.
FT DOMAIN 573..674
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 685 AA; 74796 MW; E1A68E055C848931 CRC64;
MPDLLIELFS EEIPARMQGR AADDLKKLMT DGMVEAGLTY ASAAAFSTPR RLCLTVEGLL
AESPTVREER KGPKVGAPDK AIEGFLRGAG LTRDKLEERD TSKGAVYFAS FEKQGRPAPE
IIAEVLEQTI RTFPWPKSMR WGTGSLRWVR PLHSILCVLS DEASSEVVPL DVDGITSGKA
TYGHRFMAPN QITVNGFEDY EAQLKRAFVV LNAGERADAI WEDAKNQAFA NGLEVVEDAG
LLREVAGLVE WPVVLMGEIA EDFLGLPPEV LQTSMKEHQK FFSVKNAKTG RIERFITVAN
RETVDNGATI LAGNQKVLFA RLSDAKFFWE NDLRVATSDM ASWTAALSNV TFHNKLGTQA
ERIERIAALA RELAPVVGAD ADEAERAAKL AKADLSSEMV YEFPELQGLM GRYYAEAAGE
TAAVAAAAEE HYAPLGPSDA VPTAPVSVAV SLADKIDTLT GFWAIDEKPT GSKDPFALRR
AALGIIRLVL ENDLTIRSKP LFTKADMRAD SDDLLSFFHD RLKVYLRDQG VRHDVIDACI
AMEGNDDLAL LVKRAVALEA FLKTEDGTNL LQGFKRANNI LSKEEDKDGV EYSYGGDVKF
AETEEERALF AALTAEGPAI ETALKAEDFA GAMSGMAGLR APIDAFFEAV QVNSDNQTVR
RNRLNLLSDI RKLVGSVADL SRVEG
//
