SYGB_ALISL
ID SYGB_ALISL Reviewed; 688 AA.
AC B6EGT3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=VSAL_I2965;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
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; FM178379; CAQ80649.1; -; Genomic_DNA.
DR RefSeq; WP_012551367.1; NC_011312.1.
DR AlphaFoldDB; B6EGT3; -.
DR SMR; B6EGT3; -.
DR STRING; 316275.VSAL_I2965; -.
DR EnsemblBacteria; CAQ80649; CAQ80649; VSAL_I2965.
DR KEGG; vsa:VSAL_I2965; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000001730; Chromosome 1.
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..688
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101262"
SQ SEQUENCE 688 AA; 75890 MW; E69F45D8811383C0 CRC64;
MAKNFLIELG TEELPPKALR SLAEAFAANF EAGLKAAGLA HQGIKWYATP RRLALKIAEL
DEGQADKIVE KRGPAIASAF DADGNPTKAA QGWARGNGIT VEQAERLKTD KGEWLLHKEE
VKGQPVKGLV VELAAKALAG LPIPKAMRWG NSDIQFIRPV KTLTILLGDE LIEGTILGVA
STRTIRGHRF MGESEFTIDS ADQYPAILEE RGKVMADYDA RKAIILAGAK KAAEAVGGIA
DLEDELVEEV TSLVEWPVVL TAKFEQEFLN VPSEALVYTM KGDQKYFPVY DQEKNLLPNF
IFVTNIESKE PRHIIEGNEK VVRPRLADAE FFFNTDRKRP LIDRLPELEQ AIFQKQLGTI
KDKTDRITEL AGYIAEQIGA DVEKSQRAGL LAKCDLMTSM VFEFTDTQGV MGMHYATHDG
EDAQVALALY EQYMPRFAGD DLPSTDVSAS VAMADKLDTL VGIFGIGQAP KGSDPFALRR
AALGILRIIV EKGYNLDLVD LVAKAQSLFG DKLTNANVDT DVIDFMLGRF RAWYQDEGFS
VDIIQAVLAR RPTKPADFDQ RVKAVSHFRE LDAAESLAAA NKRVGNILAK FDGELAQEID
LALLQEDAEK VLAEKVEILA EALEPVFIAG NYQEALSRLA ELREPVDAFF DGVMVMADDE
ALKLNRLTLL NKLRNLFLDI ADISLLQK