ID   A0A0S7DLP2_9EURO        Unreviewed;       666 AA.
AC   A0A0S7DLP2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE            EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033033};
GN   ORFNames=ALT_000453 {ECO:0000313|EMBL:GIM38072.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM38072.1};
RN   [1] {ECO:0000313|EMBL:GIM38072.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM38072.1};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT   lentulus IFM 54703T.";
RL   Genome Announc. 4:e01568-15(2016).
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:0000256|ARBA:ARBA00001766};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363038}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GIM38072.1}.
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DR   EMBL; BCLY01000008; GIM38072.1; -; Genomic_DNA.
DR   STRING; 293939.A0A0S7DLP2; -.
DR   VEuPathDB; FungiDB:TMP_alenIFM54703_3775; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; cd07956; Anticodon_Ia_Arg; 1.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 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; 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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363038};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363038};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363038};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363038};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363038}.
SQ   SEQUENCE   666 AA;  74765 MW;  14E4CB56DC7B9C03 CRC64;
     MASAADLPVA VEGLTLHSTA ETSKFPNCYP SLNPVDAYRV HIAEKLGAAA GIEPEKLYPK
     LQWTNTLDKG DLVLPVPSLQ IKKNPQELCK ELAEKFPESD LVAPPVPFGV HLQFFFKPEP
     LTKTVISRIL KEKATFGTNG NQGLRDPSDP SKGKKRIIVE FSSPNIAKPF HAGHLRSTII
     GGFLANLYTV MGWDVIKMNY LGDWGKQYGL LANGFKRFGN EEELLKNPIN HLFDVYVKIN
     QIVAQQEGPI KELKEQIKAK KEKNEDVTVL EAELAKLVDV SEDEKARRYF KSMEDGDQEA
     LALWRRFRDL SIEKYKQTYA RLNIDFDVYS GESQIKNESM TAAYNAMEKA GVSEKSEGAV
     IVDFTKHGAK KLGKAIIVRK DGTPLYLTRD IGAIMERDEA YHFDKMIYVV AAQQDLHLAQ
     LFKITELMGR KDLASRCQHI NFGMVRGMST RKGTVKFLDD ILRDVADKMH EVMKGNAEKY
     AQVENPEETA DILGLTSVMV QDMTGKRING YDFNLDAMTS FEGDTGPYLQ YAHARLCSIV
     RKSGLNVEEL DSANLDLLTE PHAVDLVRLL ATWPDVLLNT TKTLEPTTIL TYLFRMTHIL
     SSSYDVLKVV GSEPELKKAR MALYEAARQV LHNGMRVLGL SPVERYVITL NLETKLGLTF
     TLFSSM
//