SYGB_HALOH
ID SYGB_HALOH Reviewed; 686 AA.
AC B8CXH5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=Hore_12440;
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562;
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(2009).
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; CP001098; ACL69994.1; -; Genomic_DNA.
DR RefSeq; WP_012636178.1; NC_011899.1.
DR AlphaFoldDB; B8CXH5; -.
DR SMR; B8CXH5; -.
DR STRING; 373903.Hore_12440; -.
DR PRIDE; B8CXH5; -.
DR EnsemblBacteria; ACL69994; ACL69994; Hore_12440.
DR KEGG; hor:Hore_12440; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000000719; 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 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; Reference proteome.
FT CHAIN 1..686
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197203"
SQ SEQUENCE 686 AA; 78940 MW; 4DA6D6BC87E9A37D CRC64;
MARDLLFEIG TEEMPAGLIG KIRSDLKDLA INTLEDKRLD FKECKVFSTP RRLVLFVKEL
AEKQEEKREV VKGPARSIAF EDDGTPTRAA KGFSRAQGVE VDDLIIKDDY VYVEKIEQGQ
DTAGLLKDIL PGLINKLPLP RSMRWADYNF KFIRPIRWLL ALFGEEIISF SMAGVQSGAY
TRGHRFLVKD RLEVKDPDHY FDVMEKGYII VDHNKRRELI LKQIREIEKE IGKVMVEDDL
LTEVVDLVEY PTAFYGKFDR SYLELPDDVL ITSMAEHQRY FPVIDEDGSL SPYFVGVRDG
IEDYIEEVRY GNEMVLRARL ADARFFFEED LKVSIEERQK ELEEIVFQED LGSMMDKVKR
LKQLVIQIGK SLNLKESQLQ SLIRAAELSK NDLVTEMVNE FTKLQGVMGR EYALINGEDE
EVATAIYEQY LPRYSGDRLP QTLYGRILSI ADKIDNITSH FSLGMIPSGS QDPFALRRQA
NGIVNIIIDA QLPLKLSSLL NWSIEVLEPG DKDFVNEEKS FLLQRLETIL DERGIRYDII
NSVVRVGDDD PNNILSRAEA VMSLRKENPD LFVDLIQGLV RARNLASKGE GNNDINPEYF
ECREEKELYD IYRKIKDEIQ RQFKKKNYLS GLKKLVDVKE PVDNFLDNVV VMVEDERIKN
NRLALLQEIS NLVSGVMNIS EIALDD