SYGB_ALKHC
ID SYGB_ALKHC Reviewed; 693 AA.
AC Q9KD48;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Glycine--tRNA ligase beta subunit;
DE EC=6.1.1.14;
DE AltName: Full=Glycyl-tRNA synthetase beta subunit;
DE Short=GlyRS;
GN Name=glyS; OrderedLocusNames=BH1371;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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;
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BA000004; BAB05090.1; -; Genomic_DNA.
DR PIR; C83821; C83821.
DR RefSeq; WP_010897536.1; NC_002570.2.
DR AlphaFoldDB; Q9KD48; -.
DR SMR; Q9KD48; -.
DR STRING; 272558.10173987; -.
DR EnsemblBacteria; BAB05090; BAB05090; BAB05090.
DR KEGG; bha:BH1371; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000001258; 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..693
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_0000072893"
SQ SEQUENCE 693 AA; 77834 MW; 30F9919712105754 CRC64;
MSKRDFLLEI GLEELPARFV SDGEKQLADK VESFLKEQRI SFEQISSFST PRRLAVLVIG
LAEKQADVEE ESRGPAKKIA LDESGNWTKA AQGFARGQGV SVDDLYIQEV KGTEYIFAKK
FVAGQETASL LPELKELITS LHFPKNMRWH TYSLRYARPI QWLVALYGQE VIPFEITGVA
AGLETAGHRF LGENVTIDEP TLYKEKLLQQ YVMADSEERK KAIRHQIQSI MEEKDWVIPI
DEDLLDEVTN LVEYPTALFG RFDEAFLSLP NEVLITSMRE HQRYFPVKNQ AGELLPYFVT
IRNGDHRHLE NIVKGNEKVL RARLSDAAFF YGEDQKLNID EANKRLDQIV YHEELGSIGD
KIKRVKVLAA SIAEKLGVTS QTLQAINRVA EICKFDLVTQ MVGEFPELQG RMGEVYAEIA
GEPPEVAKGI VEHYLPRFAG DQSPSSVQGT VVSLADKLDT IAACFGIGLI PTGSQDPYAL
RRQAAGVVQI LLDHELDLDV DELLLETVEQ LQEKELLTVP ESEVVKQLRE FFALRVKTKL
QDEGVRYDLT DAVLASGISN VPVVFKKAKL LVSKVNTPEF KELVEGLSRV TNIAGKAEKN
VAINPDLFEK EEERVLYEAY VQTKDLVQGA LASGDVSAAY AALEQTIEPI HQYFEHVMVM
VDEQVIKENR LALMHAFAGV IGSYANFQEI VFK