SYGB_SHESA
ID SYGB_SHESA Reviewed; 688 AA.
AC A0KR42;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=Shewana3_0016;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) 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; CP000469; ABK46261.1; -; Genomic_DNA.
DR RefSeq; WP_011715310.1; NC_008577.1.
DR AlphaFoldDB; A0KR42; -.
DR SMR; A0KR42; -.
DR STRING; 94122.Shewana3_0016; -.
DR EnsemblBacteria; ABK46261; ABK46261; Shewana3_0016.
DR KEGG; shn:Shewana3_0016; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000002589; 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 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_1000006407"
SQ SEQUENCE 688 AA; 75154 MW; 5D292F87BFD7593C CRC64;
MNFENLLIEL GTEELPPKAL RKLAESFLAN FTEELTKADL AFKSAVWYAA PRRLAINVTE
LALAQADKIV EKRGPAVSSA FDAEGKPTKA AEGWARGNGI TVDQAERLVT DKGEWLVYNA
KVEGVETKSL IAAMAQRALD KLPIPKPMRW GSSKTQFIRP VHTATMLLGS ELIEGELLGI
KSARNVRGHR FMGTGFELDH ADNYLTLLKE KGKVIADYES RKALIKADAE KAAAKIGGTA
DIEDDLLEEV TSLVEWPVVL TASFEEKFLN VPSEALVYTM KGDQKYFPVF DDAGKLLPNF
IFVANIESKD PAQIIAGNEK VVRPRLADAE FFFNTDKKHT LESRLPSLET VLFQQQLGTL
KDKVTRISAL AAFIAEQTGA NAVDAARAGL LSKTDLMTNM VMEFTDTQGT MGMHYARLDG
ETEAVALAME EQYKPKFSGD TVPTAAVSCA VALADKLDTL VGIFGIGQAP KGAADPFALR
RAAIGVLRII VENKLPLDLV TLIAKAQELH GTNLSNANAS DEVLEFLMAR FRAWYQDKGI
EVDVILAVLA RRPTRPADFD SRINAVSHFR SLEASSALAA ANKRVSNILA KVEGELPTTI
NSALLAEAAE QALAAKLAEL QPQLAPLFAN ADYQQALTLL ASLRESVDQF FEDVMVMADD
EALKNNRLAL LNNLREQFLH VADISLLQ