ID   SYR_MIMIV               Reviewed;         600 AA.
AC   Q5UQ59;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   Name=RARS; OrderedLocusNames=MIMI_R663;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus;
OC   Mimivirus bradfordmassiliense.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
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;
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AY653733; AAV50924.1; -; Genomic_DNA.
DR   RefSeq; YP_003987185.1; NC_014649.1.
DR   SMR; Q5UQ59; -.
DR   GeneID; 9925309; -.
DR   KEGG; vg:9925309; -.
DR   OrthoDB; 29787at10239; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..600
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151665"
FT   MOTIF           152..162
FT                   /note="'HIGH' region"
FT   BINDING         151..153
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         162
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         332
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         336
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         360
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
SQ   SEQUENCE   600 AA;  68994 MW;  8B35DBD6794CCE0E CRC64;
     MQDNLIYLAN CFLNEAIKTT LQNLNKVNII DTPELYSFVK GINTDYQFNK STKLANDCNL
     DKEKIVNELI TQLKSNSFFE NISSVELEQN KSVKINGKKT NTVIKQIMIT LNISKLYLSN
     RINLLYKRIL SGSSIYVPNT ITKKIIVDYS SPNIAKEMHI GHLRSTIIGE SICRVLEMCG
     HDVYRINHVG DWGTQFGMLI AYIKNNQIES YTISELMNIY KESRKLFESS IDFKNQSRLE
     TVSLQNGNIE SITIWQKIHK ISMNSFHEIY SLLGINNLIT KGESFYQDQM TELVNSLTSD
     NKITVENDMK LMFVEGISKP FILQKSDGGF TYDTSDLTAL KYRLFIEKAD HIIYVVDSSQ
     QEHFSQMFQI AEKLDWIKNQ QLQHIGFGLV LGSDGSKLKT RSGETIKLQD VIDNVVSHAS
     NITRELIKQK NLDWNDDDIL TISKKIAINC IKYSDLNNPR LNNYKFDINK MLNSKGNTAV
     YLMYGLARCK SILRKVPNNT VLNGDIIIEN ENSRNLLLHV LKYVEVIDQT VETMCPHYLC
     IYLYDLIGSL TKFYTTNRCL EYDNDNLIGY NANNLRIVNM VKIIISKIFE LIGLEEIEQL
//