ID   SYI_AERPE               Reviewed;        1064 AA.
AC   Q9YF67;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=APE_0374;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA79329.1; -; Genomic_DNA.
DR   PIR; E72729; E72729.
DR   AlphaFoldDB; Q9YF67; -.
DR   SMR; Q9YF67; -.
DR   STRING; 272557.APE_0374; -.
DR   PRIDE; Q9YF67; -.
DR   EnsemblBacteria; BAA79329; BAA79329; APE_0374.
DR   KEGG; ape:APE_0374; -.
DR   PATRIC; fig|272557.25.peg.286; -.
DR   eggNOG; arCOG00807; Archaea.
DR   OMA; HLGTAWN; -.
DR   Proteomes; UP000002518; 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   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
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   TIGRFAMs; TIGR00392; ileS; 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..1064
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098574"
FT   MOTIF           53..64
FT                   /note="'HIGH' region"
FT   MOTIF           603..607
FT                   /note="'KMSKS' region"
FT   BINDING         606
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1064 AA;  123482 MW;  DCB292AD67031978 CRC64;
     MGSVPRVLEG ERYDQFALES FVKSYWEENS IYRKVKEKSS RAPRKFYFLD GPPYASAKSI
     HIGTAWNKVV KDVVLRFYRM TGYNVWDKPG YDTHGLPIEV KIEQSLGVRV KREIEEKVGV
     ENFIAACKRF VDENMEAMTR QFKEIGVFMD WENPYVTYRD EYIESGWWLV KKAWEKGLLY
     KGYRVLHWCP RCETTLADYE VSEYRELEDP SIYVKFPVEG REGEYLLVWT TTPWTLPANA
     FVMAHPDMEY VKVRVGRDTL ILAKARLDHV MREAGVSEYE VLEVLKGSQL EGLRYRHPLE
     DVVDAQRELS KWHKVVMAPE AVTPHEGSGL VHSAPGHGTI DYEIAQRIGA PVVSLVDERG
     FMTEAAGKYS GLYFRGEANK AIVEDLRARG ALFHAATIVH RYPVCWRCKT PLLLRATTQW
     FVAVTRLKNQ LMREAEKVEW QPGWAKTRFM NMLRELRDWV ISRQRYWGIP LPVWRCSSCG
     YEHVVGSVEE LESMGGRRPE NLHRPWVDRV ELKCPRCGGS MKRVPDVLDV WFDSGIAFYA
     SLGYPRDRET WERLKPVDFI VEGHDQIRGW FFSLLRSGVI GFGETPYRRV LVHGFALDEQ
     GREMHKSLGN YVDFEELIAK VPRDVVRFWV LQNTVWEDLR FSWKGLDLMR RDFNVIWNVY
     AFASIYMGLD RFDPRRTSLS SVEDSLEVED RWILSRLASL KRRYLTAMED LRIHDAARAL
     RSFIIEDVSH WYLRIIRRRV WEEVDTPSKR AAYATLYKVL WEWLLMAAPL IPYTAEYLYI
     KVFREAEERP EESIHMLDMP EPEDHLIDST LEEDMEKARM VLEAILSARN EAGLKLRRPV
     RRVIIAASNP GVEGSLRRLE GLIRLMANAK EIEFAPASAL EATRIYRVEP DYGRLGPKYK
     RDMPKVLRLI EEKGGEIGRV LAEKGVYEGE YEGLPVKLTL EDVSLKAEYP EWLKVRDTPL
     GLVAVDTRLT KEEVLEGLAR DIVRRIQAMR KEAGYSVEDY VEVWIQGGED VVEAVNALKE
     YIKRETRALK LEVGEPPSGV EVLREWELDG EKVVIALKRA AASG