SYR_PARXL
ID SYR_PARXL Reviewed; 596 AA.
AC Q146I4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; OrderedLocusNames=Bxeno_A0217;
GN ORFNames=Bxe_A4245;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC EC=6.1.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR EMBL; CP000270; ABE28755.1; -; Genomic_DNA.
DR RefSeq; WP_011486598.1; NZ_CP008760.1.
DR AlphaFoldDB; Q146I4; -.
DR SMR; Q146I4; -.
DR STRING; 266265.Bxe_A4245; -.
DR EnsemblBacteria; ABE28755; ABE28755; Bxe_A4245.
DR KEGG; bxb:DR64_1922; -.
DR KEGG; bxe:Bxe_A4245; -.
DR PATRIC; fig|266265.5.peg.227; -.
DR eggNOG; COG0018; Bacteria.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000001817; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00671; ArgRS_core; 1.
DR Gene3D; 3.30.1360.70; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR005148; Arg-tRNA-synth_N.
DR InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR11956; PTHR11956; 1.
DR Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM01016; Arg_tRNA_synt_N; 1.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF55190; SSF55190; 1.
DR TIGRFAMs; TIGR00456; argS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..596
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018006"
FT MOTIF 139..149
FT /note="'HIGH' region"
SQ SEQUENCE 596 AA; 65090 MW; 350CAADC2EC5445C CRC64;
MLPAHKHTLE TLLADTVKQV ALASQGASEA AFVSPTITLE RPKVAAHGDV ACNVAMQLAK
PLRANPRQLA QQIVDALLAQ PGARDLVEAA EVAGPGFINL RLTAAAKQAV IAAVFAEKER
FGRSQRDAGK HVLIEFVSAN PTGPLHVGHG RQAALGDALS NVLASQGWDV HREFYYNDAG
VQIQTLALST QARARGLAPG DEGWPASAYN GEYIADIAKD YLNGATVAAS DGEPVTGARD
VEDLEAIRRF AVAYLRREQD MDLQAFGVKF DQYYLESSLY KEGRVEKTVA ALIAAGKTYE
QEGALWLRTT DDGDDKDRVM RKTDGTYTYF VPDVAYHVAK WERGFTKVIN IQGSDHHGTI
ARVRAGLQGL GIGIPKGYPD YILHKMVTVM RNGEEVKISK RAGSYVTVRD LIEWSGGATP
GSEVDVDLID EETIRRGRDA VRFFLISRKA DTEFVFDIDL ALKQNDENPV HYVQYAHARI
CSVIAECKAR YNMDESTLAD VDVTPLTSER AMALLNKLAE FPDMLQHAAD ELAPHAVAFY
LRDLAGEFHS FYNDKAERVL VDDAAERNAR VALLAATRQV LANGLATIGV SAPVKM