SYR_LEPBL
ID SYR_LEPBL Reviewed; 586 AA.
AC Q052J1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=LBL_1256;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L550;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(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; CP000348; ABJ78754.1; -; Genomic_DNA.
DR RefSeq; WP_011669987.1; NC_008508.1.
DR AlphaFoldDB; Q052J1; -.
DR SMR; Q052J1; -.
DR PRIDE; Q052J1; -.
DR KEGG; lbl:LBL_1256; -.
DR HOGENOM; CLU_006406_0_1_12; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
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; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..586
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000198917"
FT MOTIF 133..143
FT /note="'HIGH' region"
SQ SEQUENCE 586 AA; 66833 MW; F40E628488804D1E CRC64;
MKENETLKQI VLKSLEEGVD SLIVSFPDVE KSSLRIKIEY SRDEKFGDYS TSFSLENSKL
LKRNPIQVSK ELVEILQKRT DLFEKVDFTP PGFVNFKISP SYLLEYIEKS ILSGDHFPKV
EHPLKINLEF VSANPTGPLN IVSARAAANG DTMASLLKAI GHNVDKEFYI NDYGNQVFLL
GVSTLVRIRE IKGEFSTRQE ADDTTPIDTI LEKNILPAEG YRGEYIKDIA NALLNEPKKS
SQIETLLKEK KYRELAELCS IWTVENNLDW QRKDLDSFGV EFDNYFRERT LHESDKVLAV
MKDLERVGKI FEEDGKKIFR STEYGDDKDR VVVRDDGRPT YLLADIAYHK DKIERGYDRI
YDIWGPDHHG YISRLSGAVQ TLGYKKENFK VIISQQVNLL ESGQKVKMSK RAGSFQTMSD
LIGFLGKHGK DVGRYFFVMR SLDAPLDFDL DLAQDQSDKN PVFYLQYAHA RICSIFREVG
TESSAEAAES LEMSEERKRL LFWIARFPEE IFDSANSMEP HRVANYLQSF AKAFTGFYLG
KNNRLKDATP EVRLGLARIC LAARSVLAEG LGLIGVSAPE KMEKES