ID   SYIC_ENCCU              Reviewed;        1017 AA.
AC   Q8SQV6;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   13-SEP-2023, entry version 127.
DE   RecName: Full=Probable isoleucine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucyl-tRNA synthetase;
DE            Short=IleRS;
GN   OrderedLocusNames=ECU11_1100;
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC         isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC         Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC         ChEBI:CHEBI:456215; EC=6.1.1.5;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AL590450; CAD26020.1; -; Genomic_DNA.
DR   RefSeq; NP_586416.1; NM_001042249.1.
DR   AlphaFoldDB; Q8SQV6; -.
DR   SMR; Q8SQV6; -.
DR   STRING; 284813.Q8SQV6; -.
DR   GeneID; 860069; -.
DR   KEGG; ecu:ECU11_1100; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_1100; -.
DR   HOGENOM; CLU_001493_1_1_1; -.
DR   InParanoid; Q8SQV6; -.
DR   OMA; EIIVIHK; -.
DR   OrthoDB; 656at2759; -.
DR   Proteomes; UP000000819; Chromosome XI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033709; Anticodon_Ile_ABEc.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023586; Ile-tRNA-ligase_type2.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF19302; DUF5915; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..1017
FT                   /note="Probable isoleucine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388378"
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           609..613
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         612
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1017 AA;  117392 MW;  21B076581AA563B4 CRC64;
     MYRKNANFVE CEEEVLEYWR RNKSFERSCE RSRGREKFTF YDGPPFATGL PHYGHLLSGT
     IKDTVTRFFY QQGYDVDRRF GWDCHGLPVE YEIDKKLGIS SRAEVLEMGI GKYNAECRGI
     VMKYSSEWEA VVERLGRWVS FRDGYRTMDM TFMESVWNIF KELFSRGLIY RGFRVMPFST
     ACSTPLSNFE SNQNYKDVSD PSVLIAFPLL KPLGGYMLSL VAWTTTPWTL PSNCGLAVNP
     GFLYGVFEHK EKFYLMHVDR IGEYFKDARI LQRVSGRELE GLEYEQPFDY FEEYRKKGFF
     RVLASGFVTD TDGTGVVHCA PGFGECDYNA FVEKGLIREN DLVPCPVDEN GRYTSEVRRY
     AGRYVKDCDK AILSDIRDKV LMNQRIVHKY PFCWRSDTPL LYKLVPNWFV KVKDHVDSLL
     RNNEKINWVP PDIKYKRFHN WLENARDWSI SRNRFWGTPI PLWVTEDYSD MICIGSVGEL
     EELSGRKIDD IHREFIDGIV IHRNGREYRR VEEVLDCWFE SGSMPYAQDH WPFCKESGVD
     LGSLSVSGGE ERNKKLVKEN FPAHFIGEGL DQTRGWFYTL HVISSLLFGQ PAFLNVVVNG
     IVLAEDGRKM SKRLRNYPDP SHIFNTYGAD SLRMYLISSP VVEAENLKFS EGGVKEVLKT
     LIIPWYNSLG FYLENRDVEP DGRSLPMDGW ITASFDNFAW SLTRKMRKYE LSSVLTLALR
     FIDDLSNWYI RMYRKEIRAG HHAVLGEILK KFSIVMGPFT PFFSEYSYQS LNPGESVHFQ
     EYPVCKNGTH PFEMAKSIIA AVRRLRETNS ISLKTPLKSA TLMSSSSLYE GIKDYIDAIK
     TECNVLELLY KEEDRSMFDI TVKPNFLSLK KDKATMKKKM KVIQGLTGDQ AYSLLSSPLV
     VDGLEILRDD VLIVKKIRCE GIAQEFGDFS IIIDNTLDEG MVKMKIAREF HSYIQKLRKS
     AGLRVGDDVV VDIQCPDLKG IVSKYFDISF GSLGALSGRG EYEFDGTLYP VSLYKKL
//