ID   SYI_SACS2               Reviewed;         986 AA.
AC   Q9UXB1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Isoleucine--tRNA ligase;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucyl-tRNA synthetase;
DE            Short=IleRS;
GN   Name=ileS; OrderedLocusNames=SSO0722; ORFNames=C10_008;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=10701121; DOI=10.1139/g99-108;
RA   Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA   Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA   Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA   Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA   Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT   "Gene content and organization of a 281-kbp contig from the genome of the
RT   extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL   Genome 43:116-136(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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) (By
CC       similarity). {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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)) (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 2 subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y18930; CAB57581.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK41020.1; -; Genomic_DNA.
DR   PIR; E90220; E90220.
DR   AlphaFoldDB; Q9UXB1; -.
DR   SMR; Q9UXB1; -.
DR   STRING; 273057.SSO0722; -.
DR   EnsemblBacteria; AAK41020; AAK41020; SSO0722.
DR   KEGG; sso:SSO0722; -.
DR   PATRIC; fig|273057.12.peg.720; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   InParanoid; Q9UXB1; -.
DR   OMA; HLGTAWN; -.
DR   PhylomeDB; Q9UXB1; -.
DR   Proteomes; UP000001974; 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-KW.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
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   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..986
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098593"
FT   MOTIF           534..538
FT                   /note="'KMSKS' region"
FT   BINDING         537
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   986 AA;  114714 MW;  0177A3C31280F5A1 CRC64;
     MIKDCILRYQ RVLGKRVHDQ PGYDTHGLPI EVATEKLLGI SNKQEIIDKI GVETFINKCK
     EFALSNADKM TQNFKNVGVF MDWERPYYTL DPSYISSSWS VIKKAYEKGM LDKGTAVLHW
     CPRCETTLSD YEVSEYRDLE DPSIYVKFKI KGEKNRYLLI WTTTPWTIPS NVFVMINKDY
     DYADVEVNGE ILVIAKDRVE AVMKEASITN YKILRTYKGS ELIGIKYEHP LREFVSAQTK
     LDDFHQVVDA GNIVTLTDGT GLVHSATGHG EEDFTVGQKY GFPVVMFVND RGEFTEEGGK
     YKGLKVRDAS KAIISDLKSK NTLFFEGKIV HRYPVCWRCK TPLILRAIDQ WFIRVTKIKD
     KMLNEIEKVN WIPDWGKSRI SNMVKELRDW VISRQRFWGT PLPIWICERC NNVMVVGSKE
     ELESIAIDPV PNDLHRPWID NVRVKCNKCG GVAKRIPDVA DVWFDSGVAF FASLGKDWQE
     KWKELGPVDL VLEGHDQLRG WFFSLLRSGL ILLDRAPYTS VLVHGFMLDE QGREMHKSLG
     NYVEPSVVVE KYGRDILRLW LLRNTTWEDA KFSWKALELT KRDLQIIWNT FVFASMYMNL
     DNFEPDKYTL DDIIKYAKIE DLWILSRFNS MLKKVNESMK DYKVHEMTNY LINFLIEDVS
     RFYIRLIRKR AWIEANTQDK IAMYYILYYI LKQWIILAST IIPFISEKIY KSFVVNAKES
     VSMESSINYD ERFIDNELER AFEVAREINE ASLNARAKAG IKLRWPLAKV YIFIENEDTL
     AKVGRIKDVL ISMLNAKDIE ISKIEGFKSF SKYKVEPNRS IIGKEYKSMS PKIVEYIENN
     RDIIAMDILN KKQHVAKIDN FDIILNASYV IISEETVEGF ISSKFSKGIV VISKEISESE
     EEEGLIRDII RRIQFMRKQL KLNVLDYIEI SMKVPEERVK TIQKWEEFIK SETRASNIIL
     GEAKGDITMD WDIEGESYII GIKKST