SYGB_HAEI8
ID SYGB_HAEI8 Reviewed; 722 AA.
AC Q4QLY5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 107.
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=NTHI1093;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX87962.1; -; Genomic_DNA.
DR RefSeq; WP_011272293.1; NC_007146.2.
DR AlphaFoldDB; Q4QLY5; -.
DR SMR; Q4QLY5; -.
DR PRIDE; Q4QLY5; -.
DR EnsemblBacteria; AAX87962; AAX87962; NTHI1093.
DR KEGG; hit:NTHI1093; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000002525; 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; 2.
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..722
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006363"
SQ SEQUENCE 722 AA; 79688 MW; AED5FA2017E84441 CRC64;
MTTQNFLVEI GTEELPPKAL KTLATSFADN VEAELNQAGL SFDKIEWFAA PRRLAVKVLN
LATQQPSKEI EKRGPAVSAA FDAEGKPTKA AEGWARGCGI TVEQAERIAT DKGEWLVHRT
KIKGQPTKNL LNDIVANALA KLPIPKPMRW ADKTVQFIRP VHTVTMLLGD ELIEGEILGV
ASARTIRGHR FLGEKEFDIQ HADQYPQLLR DKGSVVADFN ERKAEILAKS QAKATALGGV
ADIEESLLEE VTSLVEYPNV LAAKFEERFL AVPAEALVYT MKGDQKYFPI YDKDGRLLPH
FIFVSNINPE DPTAIIEGNE KVVRPRLTDA EFFFKTDLKQ KLVDRLPRLE TVLFQQQLGT
LKDKTDRIEQ LAGEIAKQIG ADEAKAKRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
GEDEEVAVAL NEQYMPRFAG DELPKSLVAS AVALADKFDT LTGIFGIGQA PKGSADPFAL
RRAALGALRI IVEKNLPLDL NDIISKAFDL YKELDNERLR NAPIAKTRGG FSEYPEGYVS
FFTRGDDLVP KQKILDEVVD FMLGRFRAWY QDEGIAVDVI QAVLARRPTR PADFDARVRA
VSHFRTLDSA EALAAANKRV SNILAKAGAA IGEINLTACV EPAEKALAEA VLALRTEVQP
LIAQGDYTAV LDKLANLRAP VDSFFDNVMV NAEDPALRQN RLAILNTLQG LFLQVADISV
LQ