ID   SYI_HALSA               Reviewed;        1070 AA.
AC   Q9HN97;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=VNG_2190G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AE004437; AAG20324.1; -; Genomic_DNA.
DR   PIR; H84369; H84369.
DR   RefSeq; WP_010903625.1; NC_002607.1.
DR   AlphaFoldDB; Q9HN97; -.
DR   SMR; Q9HN97; -.
DR   STRING; 64091.VNG_2190G; -.
DR   PaxDb; Q9HN97; -.
DR   EnsemblBacteria; AAG20324; AAG20324; VNG_2190G.
DR   GeneID; 5953285; -.
DR   KEGG; hal:VNG_2190G; -.
DR   PATRIC; fig|64091.14.peg.1684; -.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   InParanoid; Q9HN97; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 4914at2157; -.
DR   PhylomeDB; Q9HN97; -.
DR   Proteomes; UP000000554; 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   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..1070
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098577"
FT   MOTIF           50..60
FT                   /note="'HIGH' region"
FT   MOTIF           606..610
FT                   /note="'KMSKS' region"
FT   BINDING         609
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1070 AA;  119902 MW;  EABADEAC91ECBDC3 CRC64;
     MSGFGDVPDQ YDPAGVEERV FSYWEAVDAY EQTVDHRADA ETFFFVDGPP YTSGAAHMGT
     TWNKTLKDAY IRYHRMQGYD VTDRPGYDMH GLPIETKVEE QLGFESKKDI QEFGEEAFIE
     ECKRFADDNL DGLQSDFQSF GVWMDWDNPY KTVDPSYMEA AWWAFSEVHD NGLVERGQRS
     ISQCPRCETA IANNEVEYED VTDPSIYVRF DLDDREGSLV VWTTTPWTIP ANQFVAVDED
     GDYQQVRATT PDGETDVLYV ASECVEDVLS AGGYSDHEIV ADHSGSDLIG WSYTPPLADA
     VPANPTDADG THEVYHGDWV EADRTGLVHS APGHGEEDFE RGAELDLPVF CPVGEDGVYT
     DAGGKYAGAF VRDANDDIIA DLEARDAMLA SQTVEHSYGH CWRCDTGIIQ IVTDQWFITI
     TDVKDELLAN MDTSEWHPEW ARDNRFRDFV ENAPDWNVSR QRYWGIPVPI WTPEDWSGDA
     EDVLVVGTRE ELAALADQDV DPASVDLHKP TVDDITITED GTEYTRVPDV FDVWLDSSVA
     SWGTLNYPEQ EDDFDELWPA DLIMEAHDQT RGWFWSQLGM GTAALGDVPY EEVLMHGYAN
     MPDGRGMSKS KGITIEPNEV IDEYGADPMR MFLLSVTPQG DDMSFSWDET ENMQRDLNIL
     WNVFRFPRPY MALDDFDANV PAAFGGDDAG VGIADADLET VDEWLLSRLQ HVKADATAHW
     EDFEQHRALD AVLEFVVEDL SRYYVQVVRE RMWEDDASAS KTAAYATMQR VLLEVVALLA
     PYAPFVTEEL YSHLTGDRGY DTVHMADWPT VEESLRAPAL EADVAVLRAA EEAGSHARQQ
     AGRKLRWPVT RVVVDAAEDS VVDALDAHGD LLADRLNTRA IEVVEPGAAW DELAYSARAD
     MSELGPAFGD DAGAVMNALN DARVTDRDID ALAEQVAADL GRDDIELTTE MVEFVEETPE
     HVAGAAFETE TAAGTVYVDT ELNEDVESEG YAREVVRRVQ EMRKEMDLAM DAEIRLDVLV
     FDERVGELVA RHEPLITAET RARELGEVED GHREEWDVEG TTMILEVEAV