SYGB_HAEIE
ID SYGB_HAEIE Reviewed; 688 AA.
AC A5UDE3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=CGSHiEE_07355;
OS Haemophilus influenzae (strain PittEE).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374930;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittEE;
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
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; CP000671; ABQ98794.1; -; Genomic_DNA.
DR RefSeq; WP_005686190.1; NC_009566.1.
DR AlphaFoldDB; A5UDE3; -.
DR SMR; A5UDE3; -.
DR KEGG; hip:CGSHiEE_07355; -.
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_1000006364"
SQ SEQUENCE 688 AA; 75616 MW; 9C38C97948978128 CRC64;
MTTQNFLVEI GTEELPPKAL KTLATSFADN VEAELIQAGL SFDKIEWFAA PRRLAVKVLN
LATQQPSKEI EKRGPAVSAA FDAEGKPTKA AEGWARGCGI TVEQAERIAT DKGEWLVHCA
KIEGQPTKNL LNDIVANALA KLPIPKPMRW ADKTVQFIRP VHTVTMLLGD ELIEGEILGV
ASARTIRGHR FLGEKEFEIQ HADQYPQLLR EKGSVVADFN ERKAEILAKS QAKATALGGV
ADIEESLLEE VTSLVEYPNV LAAKFEERFL AVPAEALVYT MKGDQKYFPI YDKDGKLLPH
FIFVSNINPE DPTAIIEGNE KVVRPRLTDA EFFFKTDLKQ KLVDRLPRLE TVLFQQQLGT
LKDKTDRIEQ LAGEIAKQIG ADEAKAKRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
GEDEEVAVAL NEQYMPRFAG DELPKSLVAS AVALADKFDT LTGIFGIGQA PKGSADPFAL
RRAALGALRI IVEKNLPLDL EDLVKKSAAL FSDKLTNKNV VADVVDFMLG RFRAWYQDEG
IAVDVIQAVL ARRPTRPADF DARVRAVSHF RTLDSAEALA AANKRVSNIL AKADAAIGEI
NLTACVEPAE KALAEAVLVL RTEVQPLIAQ GDYTAVLDKL ANLRAPVDSF FDNVMVNAED
PALRQNRLAI LNTLQGLFLQ VADISVLQ