SYGB_CERS1
ID SYGB_CERS1 Reviewed; 697 AA.
AC A3PH07;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00255};
GN Name=glyS {ECO:0000255|HAMAP-Rule:MF_00255};
GN OrderedLocusNames=Rsph17029_0507;
OS Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=349101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17029 / ATH 2.4.9;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029.";
RL Submitted (FEB-2007) 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:0000255|HAMAP-Rule:MF_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
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DR EMBL; CP000577; ABN75623.1; -; Genomic_DNA.
DR RefSeq; WP_011840400.1; NC_009049.1.
DR AlphaFoldDB; A3PH07; -.
DR SMR; A3PH07; -.
DR EnsemblBacteria; ABN75623; ABN75623; Rsph17029_0507.
DR GeneID; 57469200; -.
DR KEGG; rsh:Rsph17029_0507; -.
DR HOGENOM; CLU_007220_2_1_5; -.
DR OMA; LPIPKRM; -.
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 PANTHER; PTHR30075; PTHR30075; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR TIGRFAMs; TIGR00211; glyS; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..697
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101325"
SQ SEQUENCE 697 AA; 75665 MW; 87CB19DA4CADB376 CRC64;
MPDLLIELFS EEIPARMQAR AREDLKKLVT DGLVEAGLTY ASAGAFSTPR RLVLSVEGLS
AESPTLREER KGPKADAPAA AIEGFLRSTG LTRDRLETRE DKKGAVLFAV VEKPGRPAPE
IVAEVLERTI RTFPWPKSMR WGTGSLRWVR PLQSILCLLS DEGGAEVVPM TLDGLTAGNS
TEGHRFMAPA RFAVSGFEDY RAKLGRAFVM LDASEREQAI WHEATTQAFA QGLEVVPDAA
LLSEVAGLVE WPVVLMGAIG EDFLGLPPEV LQTSMREHQK FFSVTNPATG RIEKFVTVAN
RETADHGETI LKGNGKVLSA RLSDARFFWE NDLRTVKTAG LEGMAEGLKQ VTFHNRLGSQ
ADRIARIEAL AREIAPLVGA SPDLAAEAAR VAKADLQSAM VGEFPELQGT MGSYYARAAG
LPEAVAQACK AHYQPLGPSD AVPTDPVSVA VALADKIDTL AGFWRIGEKP TGSKDPFALR
RAALGVIRLL LTNNSRAGLM GIMLPAMNRH LEPFDTSDFT PYERELLSFF HDRLKVHLRE
QGIRHDVIDA CLAMPGNDDL TLLVKRAEAL SAFLKTDDGT NLLQGFKRAN NILTQAEAKD
GVEYSFGADP KFAETDAERA LFAALETAEA AIGPALQAED FAAAMSAMAA LRAPIDAFFE
TVQVNADNAV LRRNRLNMLH SIRATCARVA DLTRIEG