SYGB_RICPR
ID SYGB_RICPR Reviewed; 665 AA.
AC Q9ZCB1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 109.
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=RP849;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA15273.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ235273; CAA15273.1; ALT_INIT; Genomic_DNA.
DR PIR; A71647; A71647.
DR RefSeq; NP_221197.2; NC_000963.1.
DR AlphaFoldDB; Q9ZCB1; -.
DR SMR; Q9ZCB1; -.
DR STRING; 272947.RP849; -.
DR EnsemblBacteria; CAA15273; CAA15273; CAA15273.
DR KEGG; rpr:RP849; -.
DR PATRIC; fig|272947.5.peg.887; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_1_5; -.
DR Proteomes; UP000002480; 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..665
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_0000072924"
SQ SEQUENCE 665 AA; 76216 MW; A193D931CE7463F5 CRC64;
MVSELLLELF SEEIPAFMQK NAEEGYLKIF TKIFEENEIF AKVQVFAGPR RITLHATHVP
KVILPKEEEI KGPSIEAPEI AINGFCKAHN VSKLDLSTKL RNNKLYYFFV KKTKERETKE
ILPKIIIDAI NKYSWTKSMF WGCYKIKWIR PLRNILCIFD GEILPLRFGH LSTNNITYGH
RLTNNKKLEI IDFENYRNKL LENNVILERL KREEIIKVGL LELANAQNLN IKQDVCLIEE
VTGLSEFPIV LLGKIPQKFL ELPEEVIVSV MRTHQKYFCL FDKNGSFAPY FLFVINGRFV
NTELIIQGNE KVLSARLADA LYFYKNDIAK TLESRLDKLK SVIFHTKLGS LKEKVDRITD
ICRYIAPDNI DLIMAAKLCK SDLVSDMVGE FPDLQGIMGY YYAKHEELNE EVAKAIRDHY
KPQGLNDNVP SGNATLLALA DKLDSLVGLI IVGETPNGSG DPYALRRQAL GIIRIIIENK
LEINFINLIS FSVSLYKVSS NSHLDSVISF FEERAKFYFK NDYDITLINA VLDLNLVDTK
FKLDTLKEFL VQDVGKQLLN AYKRVSNIMG NQKITGLVDA SLFSTQYEKE LFEVIQKISQ
QIIVIIANKD YQKALNLLSS LLKPITSFFD NVLVNDSDPK IAQNRLSLLQ NTCEVFDKVA
KFCRL