SYGB_SHEB8
ID SYGB_SHEB8 Reviewed; 689 AA.
AC A6WH92;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=Shew185_0008;
OS Shewanella baltica (strain OS185).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=402882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS185;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS185.";
RL Submitted (JUL-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; CP000753; ABS06181.1; -; Genomic_DNA.
DR RefSeq; WP_011981989.1; NC_009665.1.
DR AlphaFoldDB; A6WH92; -.
DR SMR; A6WH92; -.
DR KEGG; sbm:Shew185_0008; -.
DR HOGENOM; CLU_007220_2_2_6; -.
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 SMART; SM00836; DALR_1; 1.
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_1000006401"
SQ SEQUENCE 689 AA; 75146 MW; B15CEB83467407A7 CRC64;
MNFENLLIEL GTEELPPKSL RKLAESFLAN FTEELTKADL AFSSAVWYAA PRRLAINVTE
LALAQADKVV EKRGPAVSSA FDAEGKPTKA AEGWARGNGI TVEQAERLVT DKGEWLVHNA
KVEGVETKSL IAAMAQRALD KLPIPKPMRW GNNKTQFIRP VHTATMLLGS ELIEGELLGI
KSARTVRGHR FMGQASFELA HADHYLADLK EKGKVIADYE VRKTLIKADA EKAAAKIGGK
ADIEDSLLEE VASLVEWPVV LTASFEEKFL NVPSEALVYT MKGDQKYFPV FDEAGKLLPN
FIFVTNIESK DPAQIISGNE KVVRPRLADA EFFFNTDKKH TLESRLPSLE TVLFQQQLGT
LKDKVNRISA LAAFIAEQTG ANAVDAARAG LLSKTDLMTN MVMEFTDTQG TMGMHYARLD
GETEAVAVAM EEQYKPKFSG DTVPSAGVSC AVALADKLDT LVGIFGIGQA PKGAADPFAL
RRAAIGVLRI IVENKLPLDL VDLIAKAQAL HGTNLSNANA SDEVLEFLMA RFRAWYQDKG
IGVDVILAVL ARRPTRPADF DSRINAVSHF RSLEASSALA AANKRVSNIL AKVEGALPTT
INANLLTEAA EQALAAKLNE LQPLLAPLFA NADYQQALTL LAGLRESVDQ FFEDVMVMAD
DEALKNNRLA LLNNLREQFL HVADISLLQ