SYR_CLOPE
ID SYR_CLOPE Reviewed; 565 AA.
AC Q8XJU2;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 110.
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=CPE1661;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB81367.1; -; Genomic_DNA.
DR RefSeq; WP_011010560.1; NC_003366.1.
DR AlphaFoldDB; Q8XJU2; -.
DR SMR; Q8XJU2; -.
DR STRING; 195102.gene:10490925; -.
DR PRIDE; Q8XJU2; -.
DR EnsemblBacteria; BAB81367; BAB81367; BAB81367.
DR KEGG; cpe:CPE1661; -.
DR HOGENOM; CLU_006406_6_1_9; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000000818; Chromosome.
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..565
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151551"
FT MOTIF 120..130
FT /note="'HIGH' region"
SQ SEQUENCE 565 AA; 64626 MW; 2626BD869B6ED66E CRC64;
MDYKKLVAER IKEHVDLELE NIEKLIEIPP KPEMGDFAFP CFQLAKVMRK APNMIAAELA
EKINKEGFER VECLGPYLNF FVDKVAFSKN IISKVLEEGD KYGSSKIGEG KNVVVEYSSP
NIAKPFHVGH LFTTAIGHSL YRMLNFEGYN PIRINHLGDW GTQFGKLISA YKRWGNEEAL
EEAPINELLR IYVKFHDEAE NNPELEDEGR MYFKKLEDGD QEAVALWERF KDLSLKEFNK
IYDMLGVDFD SWAGESFYND KMDKVVEELE KANILTESNG AKVVMLDEYN MPPCIVVKSD
GASIYATRDL AAASYRHKTY NFDKCIYVVG KDQILHFNQV FKTLELAGNE WAKNCVHIPF
GLVKFADRKL STRKGNVVLL EDLLNEAIDK TRETIEEKNP QLENKEEVAK KIGIGAILFT
YLKNSRERDI VFDWKEMLSF DGETGPYVQY SYARAKSILR KAEEQKITAE PDFTKLTSKE
EFELAKTLEG LQKAVILGID KLEPSVVTRY SIEVAKAFNK FYNNHTVLNV EDEGLKAARL
ELIKATAQVI KNALFLIGID VVEKM