SYGB_ALIFM
ID SYGB_ALIFM Reviewed; 688 AA.
AC B5FEW0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=VFMJ11_0016;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-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; CP001139; ACH65158.1; -; Genomic_DNA.
DR RefSeq; WP_012532856.1; NC_011184.1.
DR AlphaFoldDB; B5FEW0; -.
DR SMR; B5FEW0; -.
DR EnsemblBacteria; ACH65158; ACH65158; VFMJ11_0016.
DR KEGG; vfm:VFMJ11_0016; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000001857; Chromosome I.
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..688
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101370"
SQ SEQUENCE 688 AA; 76055 MW; 375D4B9DFD5175DF CRC64;
MAKNFLIELG TEELPPTALR SLAEAFASNF EAELKAADLA HQGVKWYATP RRLALKVAEL
AESQADKVVE KRGPAVSAAF DADGNPTKAA QGWARGNGIT VEQAERLKTD KGEWLLHKEE
VKGKPVQELV VDFAAKALAG LPIPKAMRWG NSDIQFIRPV KTLTILLGDE LIEGSILGVS
SARTLRGHRF MGESEFTIDS ADQYPAILEE RGKVMADYDA RKAIILADSE KAAAAVGGKA
DLEDDLVEEV TSLVEWPVVL TAKFEEEFLK VPSEALVYTM KGDQKYFPVY DENKKLLPNF
IFVSNIESKE PRHVIEGNEK VVRPRLADAE FFFNTDRKRP LIDRLPELEQ AIFQKQLGTI
KDKTDRITEL AGYIAEQIGA DVEKSQRAGL LAKCDLMTSM VFEFTDTQGV MGMHYATHDG
EDEQVALALY EQYMPRFAGD DLPSTDISAS VAMADKLDTL VGIFGIGQAP KGSDPFALRR
AALGVLRIIV EKEYNLDLVD LVAKAQSLFG DKLSNANVAT DVIDFMLGRF RAWYQDEGFS
VDIIQAVLAR RPTKPADFDK RVKAVSHFRE LDAAESLAAA NKRVGNILAK FDGELAQEID
LALLQEDAEK ALAEKVEILA EALEPVFAAG NYQEALSRLA ELREPVDAFF DNVMVMADDE
ALKTNRLTLL NKLRNLFLDI ADISLLQK