SYGB_DESVM
ID SYGB_DESVM Reviewed; 701 AA.
AC B8DPG1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=DvMF_0291;
OS Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=883;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19637 / Miyazaki F;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA Richardson P.;
RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL Submitted (OCT-2008) 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; CP001197; ACL07248.1; -; Genomic_DNA.
DR RefSeq; WP_012611442.1; NC_011769.1.
DR AlphaFoldDB; B8DPG1; -.
DR SMR; B8DPG1; -.
DR STRING; 883.DvMF_0291; -.
DR EnsemblBacteria; ACL07248; ACL07248; DvMF_0291.
DR KEGG; dvm:DvMF_0291; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_7; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
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..701
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197181"
SQ SEQUENCE 701 AA; 75179 MW; DAB1C3580E328DA4 CRC64;
MSQFVLEIGF EELPSRFLPG LERELAERFA RALDDDGVEH ESIRVLTTPR RAAVLIEGIN
PVQREAEEVV PGPPVRVAFD AEGKPTKAAE GFARTQGVDM ADIFTLSTDK GEYIAVRKRT
GGANAADLIA TACPTVVAAL PFPKRMRWGS GDFTFGRPLR WLLALFDDAV VPFEVGGVVS
GGVTWGHRIH GAGPLVVKSA DDYLNVVIEK GGVTPDPAER RAMILAGGNA AAEAAGGRIL
WKESLLDEVQ GLAEHPVPLL GDIDPSFLEL PREVLLTSME SHQKSFGVEG PDGALLPHFL
TVLNLTPLDV ALVKKGWERV LRARLEDGRF FWKTDLAASF DAWLAELDNV IFLGPLGSMG
DKTRRLEKLC AWLAKAAGVA DESACARAGR LSKADLVSEM VGEFDTLQGI MGGIYARRMG
EPETVAAALA EQYLPAGPDS PVPATLAGAL LSIADKADTM AGCFGLGMIP TGAADPYALR
RCALGIARIV LEHGLRIDVR ELFRTALALY GERAWKLAPA EALVKLEEFF MARLKNHFMA
AGHETLLVEA ALAADTPEGA GIDVRAAGAR LAALSDFSRR DDFGSAVLTF KRAANIIRKQ
GQEGGAVLDG AYSHALLAED AEKALAARLE EVAPRFDALW AADDFASLFG LLGELRPAVD
AFFDGVMVMC DDAAVRTNRL NLLKALTLRL GRLADFGALQ M