ID   SYI_PYRAE               Reviewed;         981 AA.
AC   Q8ZWU4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=PAE1617;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL63605.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZWU4; -.
DR   SMR; Q8ZWU4; -.
DR   STRING; 178306.PAE1617; -.
DR   EnsemblBacteria; AAL63605; AAL63605; PAE1617.
DR   KEGG; pai:PAE1617; -.
DR   PATRIC; fig|178306.9.peg.1193; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   InParanoid; Q8ZWU4; -.
DR   OMA; HLGTAWN; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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; 2.
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.
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..981
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098587"
FT   MOTIF           50..60
FT                   /note="'HIGH' region"
FT   MOTIF           604..608
FT                   /note="'KMSKS' region"
FT   BINDING         607
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   981 AA;  114759 MW;  6F7A1242CC105D41 CRC64;
     MPHGDLPLPP SYRPHEVKKA VEEFWRRNRI FEKWKSWRGG PKFTFLEGPP TTNGMPHVGH
     IRGRTYKDVV IRFYRLLGYD VWVQGGWDMQ GMPVEWEVEK KLKLRSKKDI EQFGLEKFAL
     ECNSLVEEYL AYWREWGTKR LGLWLDLENA YETRQPHYLQ YAWRIVKRAH ELGLLTEDYR
     VLWFCPRCET SLSDHEVALG YDEREDPSIY VKFRVEGGVD EYLVIWTTTP WTIVDNEAVA
     VHPDYVYAKV EVEVGGRREY WWLAEALVPS LMAKFGIKTW RVVETKKGVE LAGVRYIHPL
     AEEVPERASR PHQVVTAEFV TLEQGTGLVH IAPGHGPEDF ELAKKYGLPV TNSVEINGIY
     NELGGRYKGK HVYDVDKEVT RDLRSKGLLV FEEKIRHEYP HCWRCGSKLI LRADRQWFIA
     ISRIRDKMYA ELQKVNVVPT KLRDRFDIFV QNARDWNISR SRVWGTPLPV WRCKKDGRIL
     VIGSLEELKK LAKELPPVDD FKLVHRPWID QVKISAHDCD EWVREPYVMD VWLDSGIAWI
     AAVDGENNRD LWEKLFPYDF VTEGIDQTRG WFYSLLATSV LYTGRAPYKN VLIQGLILDK
     HGQKMSKSKG NVIWAKDLFE KYGADPVRLY ILSKVAPWED LSFDPDEVKY VIGDLNILWN
     VVKFADTYMS LDGFDAEKYP LSQWLEKGLE EDKWILSELN IMISEFTNFV KNFEFHKAAA
     LWREFVVETL SHRYIRLLRR RVWSEEPSPD KYAAYAVLHD VLKKVLILGS ILVPFITEYL
     WQAYVRKYEK NAPESVHLAQ YPAAGSYDKE LIYAYRELFA VFSALAEARN KAGIKLRWPI
     REAYVNGAKY AERYTELLKY LGNVKEVKVG RRPDYLCVKE GELEVCVPDK IEPELYYEAL
     ARELIRRIQV MRKETGLEIS DEIHVVVETN SDDIKKAVEQ YRDYIARETR AVKLIIDAVS
     QGKEWDISGE KVKIEIRKAQ A