ID   SYI_WOLPM               Reviewed;        1111 AA.
AC   Q73HW7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02003};
GN   Name=ileS {ECO:0000255|HAMAP-Rule:MF_02003}; OrderedLocusNames=WD_0423;
OS   Wolbachia pipientis wMel.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=163164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA   Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C.,
RA   McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA   Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA   Nelson W.C., Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R.,
RA   Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA   O'Neill S.L., Eisen J.A.;
RT   "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT   streamlined genome overrun by mobile genetic elements.";
RL   PLoS Biol. 2:327-341(2004).
CC   -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS
CC       can inadvertently accommodate and process structurally similar amino
CC       acids such as valine, to avoid such errors it has two additional
CC       distinct tRNA(Ile)-dependent editing activities. One activity is
CC       designated as 'pretransfer' editing and involves the hydrolysis of
CC       activated Val-AMP. The other activity is designated 'posttransfer'
CC       editing and involves deacylation of mischarged Val-tRNA(Ile).
CC       {ECO:0000255|HAMAP-Rule:MF_02003}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02003};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02003};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- DOMAIN: IleRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated valine is translocated from the
CC       active site to the editing site, which sterically excludes the
CC       correctly activated isoleucine. The single editing site contains two
CC       valyl binding pockets, one specific for each substrate (Val-AMP or Val-
CC       tRNA(Ile)). {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02003}.
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DR   EMBL; AE017196; AAS14146.1; -; Genomic_DNA.
DR   RefSeq; WP_010962579.1; NC_002978.6.
DR   AlphaFoldDB; Q73HW7; -.
DR   SMR; Q73HW7; -.
DR   STRING; 163164.WD_0423; -.
DR   EnsemblBacteria; AAS14146; AAS14146; WD_0423.
DR   GeneID; 29555413; -.
DR   KEGG; wol:WD_0423; -.
DR   eggNOG; COG0060; Bacteria.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008215; Chromosome.
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-UniRule.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
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   PANTHER; PTHR42780; PTHR42780; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; SSF47323; 2.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN           1..1111
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098572"
FT   MOTIF           52..62
FT                   /note="'HIGH' region"
FT   MOTIF           645..649
FT                   /note="'KMSKS' region"
FT   BINDING         648
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1111 AA;  128833 MW;  A8673A51D27841F7 CRC64;
     MKSKHYPDTV SSPDFLSLEK EIIKFWQENK VFERSVEERS KDNCFVFYDG PPFANGLPHY
     GHLLTGFIKD AFARYQTMLQ KRVERRFGWD CHGLPAEMGA EKELGISGRT EIEKFGIDKF
     NDHCRTSVMK FSSEWEKYVN RQARWVDFHN DYKTMDKSFM ESVMWAFKQL YDKGLVYESV
     RVVPYSWACE TPLSNFETRL DNAYREKVSK AVTVAFELLE NPQQFKSVKR KCKLLAWTTT
     PWTLPSNLAL AIGKDIKYCA VSVHPLMSFQ RVTLESISGS QCLGTGMTGS SEGSSMNGEI
     YIFAESYLEK FISHSEQNNI PYENCNIKLK ANDLAGLSYK PLFDYFKDTK NAFRVFIADY
     VTEEDGTGVV HTAPGFGEED FYLCQSHDIP VICPIDNSGK FTAEVSDLAG VHVFDANDTV
     IKKLKGQGSW FKTEQYIHNY PHCWRTDTPL IYRTMPSWYV AVTKFKSRMV ELNKRVNWIP
     NHIRDGQFGK WLEGAHDWSI SRNRFWGTPI PVWKSDDARY PRVDVYGSIE ELERDFNVKI
     DDLHRPFIDT LTRLNPDDPT GKSVMRRVPD VFDCWFESGS MPFAQIHYPF ENKEWFESAD
     FITEYIAQTR GWFYTLFVLS TALFNREPFK NCICHGVVLD VKGQKLSKRL NNYADPMEVF
     DRYGSDALRF LMLSGSIICG GNLLLDKEGN SIRDVLKNVI KPIWNSYHFF TMYANADGIK
     AEVCKDYQST IDRYMISKCF EAVESIQASM NSYSSQEACK ILIDFFEVLN NWYIRRSRER
     FWKSDLDQDK TDAYNVLYTV FYYILRAAAP LLPLITENIW QGLKYEETSV HLANFPQLEK
     FDSQLIAKMD LVREVCNSAL SIRNTFNIRI RQPLGSMIIY HQSSCSFLEG EPLSVIPEFF
     PVIQVADTGI QCAADSNEYQ EMIKDEVNVK SLELVNRLEG IASLELKLNF PLLGKRIPDK
     IKKLVQYVKE GKWKQVENEQ IFLGDESENY IIEKGEYELL LKANSEYSSV FDNNKGIVIL
     NTELNDELIL EGLARDVVRL IQETRKQADF HISDRIRVII KTEEEKIKEA INTWFEYIKE
     QTLALSLDIN TEIGTNFYSK EYQDLSVSIE R