SYGB_DESHD
ID SYGB_DESHD Reviewed; 690 AA.
AC B8FUJ0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=Dhaf_4254;
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2;
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
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; CP001336; ACL22260.1; -; Genomic_DNA.
DR RefSeq; WP_005816394.1; NC_011830.1.
DR AlphaFoldDB; B8FUJ0; -.
DR SMR; B8FUJ0; -.
DR EnsemblBacteria; ACL22260; ACL22260; Dhaf_4254.
DR KEGG; dhd:Dhaf_4254; -.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000007726; 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.
FT CHAIN 1..690
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197176"
SQ SEQUENCE 690 AA; 76754 MW; 0BEBE430DEE023FB CRC64;
MAKDFLLEIG TEEIPAKFAP GVLNQLREQA QKYCQELRLD 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
VRNGDDYALA KVKAGNEKVL KARLEDAAFY YREDQKTPLA ELVEKLDKVT YHEKLGSVRQ
RVERIRTLAR GIAARLGMES EKQDLVERTA 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