SYGB_DESHY
ID SYGB_DESHY Reviewed; 690 AA.
AC Q24SX0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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}; OrderedLocusNames=DSY3083;
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE84872.1; -; Genomic_DNA.
DR RefSeq; WP_011460837.1; NC_007907.1.
DR AlphaFoldDB; Q24SX0; -.
DR SMR; Q24SX0; -.
DR STRING; 138119.DSY3083; -.
DR EnsemblBacteria; BAE84872; BAE84872; DSY3083.
DR KEGG; dsy:DSY3083; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000001946; Chromosome.
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; Reference proteome.
FT CHAIN 1..690
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101272"
SQ SEQUENCE 690 AA; 76701 MW; 71F9F9A773A41CDC CRC64;
MAKDFLLEIG TEEIPAKFAP GVLNQLREQA QKHCQELRLD YQDLKVYTTP RRFAVLIQGL
AEKQTDFTAE VKGPAVKAAY DAEGNPTKAA QGFARGQGVE PKDLFVQELN GVSYVYARKF
ELGQPTLQLL PKLCTDLITG LHFPKPMRWA DLEFRFARPI RWIVALFGSE VIPFEFVGLA
SGKASRGHRT LGGPVTLDSP ADYEKQMLQA FVMVDPEQRR QSVWEQIHAL AAKVGGDVEK
DDDLLDEVTH IIEYPTALLG EVAPNYMHLP EPVITTPMKE HQRYFPVRDK EGKLLPYFIT
VRNGDDHALA KVKAGNEKVL KARLEDAAFY YREDQKTPLA ELVEKLDKVT YHEKLGSVRQ
RVERIRTLAR GIAARLGMES KKQDLVERTA LLAKADLVTL MVYDFPELQG IMGADYARMV
GEKPEVCTGI LEHYQPRFAG DELPQSYTGQ IVSVADKLDA IVGAFGIGIQ PTGSQDPYAL
RRQAQGVVGI ILEAGWDISL EQLIAASYVN FAEQGISLLP LADLQSALQD FFQQRLRFVL
QEQGARYDTL DAVLAQGSNQ ITRAARKAQV LAAKRETTEF VPYSQAYIRC LNLSKKAQTQ
PLDPKNLIDP TEIALAAALV QRQEAFAALI EKGDYAEAYA LASELIPMIE ALFNAVMIMV
EDEILKQARL ALLGECVAIL GCLGDLSLLA