SYGB_GLAP5
ID SYGB_GLAP5 Reviewed; 689 AA.
AC B8F711;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=HAPS_1559;
OS Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Glaesserella.
OX NCBI_TaxID=557723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH0165;
RX PubMed=19074396; DOI=10.1128/jb.01682-08;
RA Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA Jin M., Jin Q., Chen H.;
RT "Complete genome sequence of Haemophilus parasuis SH0165.";
RL J. Bacteriol. 191:1359-1360(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; CP001321; ACL33113.1; -; Genomic_DNA.
DR RefSeq; WP_015939829.1; NC_011852.1.
DR AlphaFoldDB; B8F711; -.
DR SMR; B8F711; -.
DR STRING; 557723.HAPS_1559; -.
DR EnsemblBacteria; ACL33113; ACL33113; HAPS_1559.
DR KEGG; hap:HAPS_1559; -.
DR PATRIC; fig|557723.8.peg.1531; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000006743; 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..689
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197202"
SQ SEQUENCE 689 AA; 76027 MW; 8ABB781988A62A17 CRC64;
MTTQNFLAEI GTEELPPKAL KKLATAFAEN VEAELNQAGL SFDKVEWFAA PRRLAVKVLG
LATAQPSKEV EKRGPAVSAA FDAEGKPTKA AEGWAKGCGI TVEQAERIAT DKGEWLVHRA
VIEGQPTKNL LVGIISQALA KLPIPKTMRW GDKTEQFVRP VHTVTLLLGD ELIEGEILGV
ASGTTVRGHR FLGEREFQIS HADQYPALLK EKGSVVADFN ERKALILAKA QEKATALGGV
ADIEEDLLDE VTSLVEYPNV LAAKFEERFL AVPAEALVYT MKGDQKYFPI YDKDGKLLPH
FIFVSNINPE DPSKIIEGNE KVVRPRLTDA EFFFKTDLKQ RLEDQLPRLE TVLFQQQLGT
LRDKTARIEQ LAGEIAKQIG ADETKAKRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
GEDEEVAVAL NEQYMPRFAG DELPKSLVAS SVALADKFDT LTGIFGIGQA PKGSADPFAL
RRAALGALRI IVEKNLPLDL SDLVATSAKL FGDKLTNSNV VEEVVDFMLG RFRAWYQDEG
IAVDVIQAVL ARRPTRPADF DARVRAVSHF RTLDSAEALA AANKRVSNIL AKVEGKISSE
IDRTLLVEAE EKALAEQVIT LQAELVPLFE KGEYQTALDR LAGLREVVDN FFDKVMVNAE
DPKLRQNRQA ILNNLRNLFL QVADISLLQ