SYGB_PERMH
ID SYGB_PERMH Reviewed; 705 AA.
AC C0QUJ3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
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=PERMA_0569;
OS Persephonella marina (strain DSM 14350 / EX-H1).
OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; Persephonella.
OX NCBI_TaxID=123214;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14350 / EX-H1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(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; CP001230; ACO03046.1; -; Genomic_DNA.
DR RefSeq; WP_012675285.1; NC_012440.1.
DR AlphaFoldDB; C0QUJ3; -.
DR SMR; C0QUJ3; -.
DR STRING; 123214.PERMA_0569; -.
DR PRIDE; C0QUJ3; -.
DR EnsemblBacteria; ACO03046; ACO03046; PERMA_0569.
DR KEGG; pmx:PERMA_0569; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_0; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000001366; 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..705
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197209"
SQ SEQUENCE 705 AA; 82014 MW; 5D6BD7A871AE7842 CRC64;
MKKYLLEIGC EELPPKAVDT AISYFKERLE GLFENFFEYR TEENISVFGT PRRIGFILSN
LREKEPSEEK TILGPPAKVG IDEKGNFTKA ALAFASKNNI PVEQLKIIEN EKGRYIGATL
IKEGKDIRTF IQEVIPDLIT KIPFPKLMRW NETGFRFSRP VRWIVSLLDN EVVSFSIAGI
DADRYTHLHR FMTTPTGRGE RKKIPDVDSY FQIMKLGFII PKYEERKEAV KTQLTGFANS
INAEPVIDED LLDEVTNLTE FPVGILGDFS PEYLILPKEV IITVCKVHQR YFNFEKDGKL
IPKFLAFSNT AVKDREKVKS GYEKVLKARL EDALFFYEED LKHNLEDFYP QLEGIQFHHK
LGSMLDKVKR NGEIAVLLSR ELNFENLKDL LRANKLSKCD LLTEMVKEFD ELQGIMGMHY
ALKQGEKEEV AKAIYEHYLP KTSDDQLPET DIGTLLSLSD KLDTVISFIS IGEKPKATAD
PFGIRRNSIG IVRILVEKGI DLDLKKLLQD ISREARKVKI LRLADIEKEW EIIFDERTIP
EILDFIEGRF IAYMKDKGFD TDIINSVVSV DSYNLYRNYL KIKSIQELKK NPEFTDIMTV
FKRVGRIIPE EFEEHFNPDT LVQDEEKELY RKYTEVNKIF SKDVEDRRYT EALNELLKMK
PFIDKFFDNV MVMTEDKKLR ENRLSLMKLI NNMFRKIADF TKITT