SYGB_SHESM
ID SYGB_SHESM Reviewed; 688 AA.
AC Q0HPC7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Shewmr4_0008;
OS Shewanella sp. (strain MR-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60480;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-4;
RG US DOE Joint Genome Institute;
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. MR-4.";
RL Submitted (AUG-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; CP000446; ABI37090.1; -; Genomic_DNA.
DR RefSeq; WP_011620845.1; NC_008321.1.
DR AlphaFoldDB; Q0HPC7; -.
DR SMR; Q0HPC7; -.
DR KEGG; she:Shewmr4_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..688
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006408"
SQ SEQUENCE 688 AA; 75140 MW; 3AA9A550A461365C CRC64;
MNFENLLIEL GTEELPPKAL RKLAESFLAN FTEELTKADL AFKSAVWYAA PRRLAINVTE
LAIAQADKIV EKRGPAVSSA FDAEGKPTKA AEGWARGNGI TVDQAERLVT DKGEWLVYNA
KVEGVETKSL IAAMAQRALD KLPIPKPMRW GSSKTQFIRP VHTATMLLGS ELIEGELLGI
KSARNVRGHR FMGTGFELDH ADNYLTLLKE KGKVIADYES RKALIKADAE KAAAKIGGTA
DIEDDLLEEV TSLVEWPVVL TASFEEKFLN VPSEALVYTM KGDQKYFPVF DEAGKLLPNF
IFVANIESKD PAQIIAGNEK VVRPRLADAE FFFNTDKKHT LESRLPSLET VLFQQQLGTL
KDKVTRISAL AAFIAEQTGA NAVDAARAGL LSKTDLMTNM VMEFTDTQGT MGMHYARLDG
ETEAVALAME EQYKPKFSGD TVPTAAVSCA VALADKLDTL VGIFGIGQAP KGAADPFALR
RAAIGVLRII VENKLPLDLV TLIAKAQELH GTNLSNANAS DEVLEFLMAR FRAWYQDKGI
DVDVILAVLA RRPTRPADFD SRINAVSHFR SLEASSALAA ANKRVSNILA KVEGELPTAI
NSALLAEAAE QALAAKLAEL QPQLAPLFAN ADYQQALTLL SSLRESVDQF FEDVMVMADD
EALKNNRLAL LNNLREQFLH VADISLLQ