ID   A0A158Q523_DRAME        Unreviewed;       493 AA.
AC   A0A158Q523;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=DME_LOCUS1196 {ECO:0000313|EMBL:VDN51223.1};
OS   Dracunculus medinensis (Guinea worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX   NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000629901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:DME_0000629901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN51223.1, ECO:0000313|Proteomes:UP000274756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; UYYG01000015; VDN51223.1; -; Genomic_DNA.
DR   STRING; 318479.A0A158Q523; -.
DR   WBParaSite; DME_0000629901-mRNA-1; DME_0000629901-mRNA-1; DME_0000629901.
DR   Proteomes; UP000038040; Unplaced.
DR   Proteomes; UP000274756; Unassembled WGS sequence.
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   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 {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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274756}.
FT   DOMAIN          374..493
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   493 AA;  56814 MW;  92FCB45DDAF4F249 CRC64;
     MEYNIFLRRI LKSDDLVATL LRSNVNRTKT VVIDYSSPNL AKRFHIGNLR STLLGRFIDS
     INRKAGNKIV SINYLGDWGR QFALIAAIWP DVKPKSLDKL TDLEKVKFYT KCYVEATNRA
     EIDGEFNRKV QKIYEEMELA MASNDLNAKI LSLWKDIRRV SLRHLKNFYK ELGVEFDEFN
     SESENVRPAH ELINNLVRIG FAKVISDKTT VVEEEQSANN IILRKSNNGT LYLSRDLASL
     MQRQKKYSAD EYVYVVDQSQ FLHFDALKKI LAKIGETDLS KKVYHLMFGR VHGLSTRKGI
     TESVEEILNH GCEIAANFIS LSKTMKIDHS KVDVAKNLSL STIIVNDLKR GRKKDYVFSF
     SDAFKMNINN GLLLQMKHSR LFSLEMRNFE LLSQCNENMS FDIDLTNNET VLLIKWLEQF
     ENVLVESYKG LEPRHLIDYL VRLAHLTGNS LAVLRVLNQP REIAVPRLLL FSAARRVLNR
     GMKLIGLEPI NQM
//