ID   SYI_WOLTR               Reviewed;        1134 AA.
AC   Q5GSS3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
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};
GN   OrderedLocusNames=Wbm0363;
OS   Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=292805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRS;
RX   PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA   Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA   Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA   Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA   Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA   Koonin E., Slatko B.;
RT   "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT   human pathogenic nematode.";
RL   PLoS Biol. 3:599-614(2005).
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; Evidence={ECO:0000255|HAMAP-
CC         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; AE017321; AAW70951.1; -; Genomic_DNA.
DR   RefSeq; WP_011256561.1; NC_006833.1.
DR   AlphaFoldDB; Q5GSS3; -.
DR   SMR; Q5GSS3; -.
DR   STRING; 292805.Wbm0363; -.
DR   KEGG; wbm:Wbm0363; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_5; -.
DR   Proteomes; UP000000534; 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   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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: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; 2.
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; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..1134
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098573"
FT   MOTIF           52..62
FT                   /note="'HIGH' region"
FT   MOTIF           656..660
FT                   /note="'KMSKS' region"
FT   BINDING         659
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1134 AA;  131811 MW;  A3EDE2284B90E9B1 CRC64;
     MKPKHYPDTI SSPDFSSLEK EIIKFWQENK IFEQSVEKRS KDNCFVFYDG PPFANGLPHY
     GHLLTGFIKD AFARYQTMLQ KKVERRFGWD CHGLPAEMGA EKELGISGRT EIEKFGIEKF
     NNYCRTSVMK FSSEWEKYVN RQARWVDFHN DYKTMDRSFM ESVIWAFKQL YDKGLVYESV
     RVVPYSWACE TPLSNFETRL DTAYRKKTSK AVTVAFELLE NPQQFKQKCK LLAWTTTPWT
     LPSNLALAIG KDIEYCAVSV HSSVSFQHVT LESREKETWI PLSRTGMTEE GTETVTEDNE
     VSLVNNEIYI FAEDYLEKFI GHCEQNNIPY ENCNTKLKAD DLAGLSYKPL FNYFKGTKNA
     FRVFIADYVT GEDGTGVVHT APGFGEEDFY LCQSHDIPAI CPIDNSGRFT AEVSDLTGIH
     VFDTNDAIIK KLKEQGNWFK TEQYIHNYPH CWRTDTPLIY RAMPSWYVAV TKFKERMIEL
     NKRVNWIPTH IRDGQFGKWL ERAHDWSISR NRFWGTPIPI WKSDNARYPR VDVYGSIAEL
     ERDFNVKVND LHRPFIDSLT RPNPDDPTGK SIMRRVPDVF DCWFESGSVP FAQVHYPFEN
     KEWFESNFPA DFITEYIAQT RGWFYTLFVL STALFDSEPF KNCICHGVVL DVKGQKLSKR
     LNNYADPMEV FDKYGSDALR FLMLSGSIVC GGNLFLNKEG SSIRDVLKNV MKPIWNSYHF
     FTMYANADGI KAEVCKDYKS TIDSYMIFKC FEAVESIQAS MSNYNSQEAC KILIDFFEVL
     NNWYIRRSRE RFWKSNLDQD KTDAYNVLYT VFYYILRAAV PLLPLITETI WQGLKYKEIS
     VHLADFPQLE RYDSELIAKM DLVREICNSA LSIRNTFNIR VRQPLGSMTV YHQSSCSFLE
     SKPLSVVIPK FSPVIPMRDT GTQKEKKWSN AEMKTSMNEY QEMIKDEVNV KELKLVNSLE
     GIASLELKLN FPMLGKRIPD KVKKLVQYVK EGKWKQVDNE QVFLGNESES YIIEKDEYEL
     LLKTNSEYSS VFGDNKGIVI LNTALDDALV LEGLARDVVR LIQEARKQAD FHISDRIRVI
     IKTEDEKIKR AINTWGEYIR EQTLSLSLEI NIEIGDNFYS KEYQDLIVGI ELNC
//