SYGB_HAEDU
ID SYGB_HAEDU Reviewed; 688 AA.
AC Q7VKG6;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=HD_1942;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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; AE017143; AAP96662.1; -; Genomic_DNA.
DR RefSeq; WP_010945689.1; NC_002940.2.
DR AlphaFoldDB; Q7VKG6; -.
DR SMR; Q7VKG6; -.
DR STRING; 233412.HD_1942; -.
DR EnsemblBacteria; AAP96662; AAP96662; HD_1942.
DR KEGG; hdu:HD_1942; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000001022; 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 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; Reference proteome.
FT CHAIN 1..688
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_0000072903"
SQ SEQUENCE 688 AA; 75649 MW; 87B5D36DCE1CB290 CRC64;
MTTENFLVEI GTEELPPKAL KKLATAFADN IQAELEQAGL AFEKIEWFAT PRRLAVKVLS
LAIAQPSKEI EKRGPAVGSA FDADGQPTKA AEGWARGCGI SVEQADRVVT DKGEWLVHRA
VVEGKPTKDL LVDMVASALA KLPIAKPMRW ADKTVQFIRP VHTVTLLLGN ELIEGEILGI
TIANVVRGHR FLGESQFQIA HADEYPQILR DKGAVIADFA ERKAIILRDA QAKAAALGGV
ADIEDDLLEE VTSLVEYPNV LVAKFEERFL AVPAEALVYT MKGDQKYFPI YDKEGNLLPH
FIFVSNINPQ DPSAIIEGNE KVVRPRLSDA EFFFKTDLKQ RLVDQLPRLE TVLFQQQLGT
LRDKTDRIEQ LSGVIAEQIG ADVQKAKRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
GEAEEVAVAL NEQYMPRFAG DALPTSLVAC SVALADKIDT LTGIFGIGQH PKGDKDPFAL
RRAALGVLRI IVEKKLPLDL VHLVEKSTGL FGDKLTNKAV VADVVDFMLG RFRAWYQDEG
IAVDVIQAVL ARRPTKPADF DARVRAVSHF RTFESAEALA AANKRVTNIL AKADIAIGEI
NLSACVEPTE RALAEAVLAL KDEVRPLIAK ANYTAVLTQL ANLRTPVDNF FDHVMVNAED
PSLRQNRLAI LSTLQSLFLE VADISLLQ