SYGB_SODGM
ID SYGB_SODGM Reviewed; 689 AA.
AC Q2NX38;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=SG0012;
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans;
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(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; AP008232; BAE73287.1; -; Genomic_DNA.
DR RefSeq; WP_011409877.1; NZ_LN854557.1.
DR AlphaFoldDB; Q2NX38; -.
DR SMR; Q2NX38; -.
DR STRING; 343509.SG0012; -.
DR EnsemblBacteria; BAE73287; BAE73287; SG0012.
DR KEGG; sgl:SG0012; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR BioCyc; SGLO343509:SGP1_RS00135-MON; -.
DR Proteomes; UP000001932; 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..689
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006416"
SQ SEQUENCE 689 AA; 76438 MW; CF2800C4BACA0912 CRC64;
MTQHTFLVEI GTEELPPKAL RALAEAFAIH ISGELDAANV RHGEVSWFAA PRRLAVKVAA
LGGAQADSDV EKRGPAIAQV FDADGNPTKA AEGWARGCGI TVSQAERLAT DKGEWLVYRA
RVKGQPVQEL LCAVVSRALG KLPIPKMMRW GDNETQFIRP VHTVTLLLDD GVIAGNVLGI
DADRIVRGHR FMGEREISLE HADQYPQVLL DRGRVMADYL QRKETIRRDA EEAAKRLGGV
ADLSESLLEE VTSLVEWPVV LTARFEEKFL AVPAEALVYT MKGDQKYFPV YDAAGNLLPH
FIFVANIESK DPQQIIAGNE KVVRPRLADA EFFFNTDHKQ RLEDRLPRLD TVLFQKQLGT
LRDKSDRIEA LSAWIAGRIG ADVPQAARAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
GEPEAVALAQ KEQYQPRFAG DALPTTLVSC AVAIADKMDT LAGIFGIGQH PKGDKDPFAL
RRATLGVLRI IVEKQLPLDL QTLTEEAVRL YGEKLTNDAV VNDVIDFMLG RFRAWYQEQG
HSVDTIQAVL ARRPTRPADF DARVRAVSYF RTLEEAASLA AANKRVSNIL AKSDDPVYKD
LQASVLKDPS EITLATHLVV LREKLQPLFE AGRYQDALVE LAALREPVDA FFDSVMVMAD
DPQVRINRLT LLAQLRKLFL QVADISLLQ