ID   SYR_ENCCU               Reviewed;         563 AA.
AC   Q8SRD8;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Arginine--tRNA ligase;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase;
DE            Short=ArgRS;
GN   OrderedLocusNames=ECU08_0550;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(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;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AL590448; CAD26360.1; -; Genomic_DNA.
DR   RefSeq; NP_597184.1; NM_001041793.1.
DR   AlphaFoldDB; Q8SRD8; -.
DR   SMR; Q8SRD8; -.
DR   STRING; 284813.Q8SRD8; -.
DR   GeneID; 859606; -.
DR   KEGG; ecu:ECU08_0550; -.
DR   VEuPathDB; MicrosporidiaDB:ECU08_0550; -.
DR   HOGENOM; CLU_006406_6_2_1; -.
DR   InParanoid; Q8SRD8; -.
DR   OMA; YEWESQY; -.
DR   OrthoDB; 463402at2759; -.
DR   Proteomes; UP000000819; Chromosome VIII.
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; -; 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   PANTHER; PTHR11956; PTHR11956; 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; SSF47323; 1.
DR   TIGRFAMs; TIGR00456; argS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..563
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000383142"
SQ   SEQUENCE   563 AA;  64253 MW;  F6E50A60D4D4BB50 CRC64;
     MFNELFRKVV EAISKASKFT PEEIAACMER SYQPKKPNVT LFLDRISPSP QEDAKELLET
     LAGANIELIE NLAIRKSSVC CDINKRAILK DVLGYIQKNR EIFGNNNVGK GKRMVVEYSS
     PNIAKIFHIG HLRTTVLGQF IVNLLRASGY ETTSINYFGD WGKQFGFVLL GYSKYGSEEE
     LEKDPLKHLF NVYVKISADA EKNPDVDSEA KEIFRMMEED KDEWCMNLWR RFRELSIEKY
     KVLYKRLNVE FDVYSGESMY NEKGKSIVET SKQIKTDEDG SKVFDLGKAG KVLVMKNDGT
     TLYITRDIAA AIERLEEYSP EKIIYVVSSE QNKHFEDLFG VLEMLGYDKD KFQHVSYGLV
     AGMSTRAGKV QLLEDIIQES TEVMKNVMMS DNNKGSFTAA EMDQTAEVLA ISTLLVMDFT
     ARRVKGYEFD IEKRARNTSG TGLYLQYAHC RLRSIETKNS NVDYNDIETI DFELIHVPKV
     LNLVYKLLWF EHVVEKCLED YEPSRIVTYL QDLASSINGA INILRVLGVD KELARARLLV
     LSSARIVLHN GLRILGATPL NKM