ID   SYI_SULIM               Reviewed;        1049 AA.
AC   C3MVH6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
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=M1425_1418;
OS   Sulfolobus islandicus (strain M.14.25 / Kamchatka #1).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=427317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.14.25 / Kamchatka #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001400; ACP38171.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3MVH6; -.
DR   SMR; C3MVH6; -.
DR   KEGG; sia:M1425_1418; -.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   Proteomes; UP000001350; 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   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42765; 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; Zinc.
FT   CHAIN           1..1049
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000216259"
FT   MOTIF           48..59
FT                   /note="'HIGH' region"
FT   MOTIF           597..601
FT                   /note="'KMSKS' region"
FT   BINDING         600
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1049 AA;  121984 MW;  6E9C7F840E1C9E40 CRC64;
     MKPLTGNYDP KKIEDEIISF WEENKIYNKL RDIVSKRREK FLFIDGPPYP SSPTPHIGTI
     WNKVIKDCIL RYERLLGKKV HDQPGYDTHG LPIEVATERL LGILNKQEII DKIGVENFIN
     KCKEFALSNA TKMTQNFKDV GVFMDWERPY YTLDPSYISS SWSVIKKAYE KGMLDKGTAV
     LHWCPRCETT LSDYEVSEYR DLEDPSIYVK FKIKGEENRY LLIWTTTPWT IPSNVFVMVN
     KDYDYADVEV NGEVLVLAKD RIEAVMKEAS ITNYKVLRTY KGSELIGVKY KHPLRDFVSA
     QTKLDDFHQV VDAGNVVTLT DGTGLVHAAT GHGEEDFLIG QKYGFPVVMF VNDRGEFTEE
     GGKYKGLKVR DASKVIINDL KSKNALFFEG KIVHRYPVCW RCKTPLVLRA IDQWFIRVTK
     IKDEMLKEIE NVNWIPDWGK SRISNMVKEL RDWVISRQRF WGTPLPIWIC EKCNNVIVVG
     SREDLESIAI DSVPNDLHRP WIDNVRVKCN KCGGVAKRIA DVADVWFDSG VAFFASLGKD
     WQEKWKELGP VDLVLEGHDQ LRGWFFSLLR SGLILLDKAP YVSVLVHGFM LDEQGREMHK
     SLGNYVEPSV VIQRYGRDIL RLWLLRNTTW EDARFSWRAL ELTKRDLQII WNTYVFASMY
     MNLDNFEPVK YTLDDVIKYA KIEDLWILSR FNSMLKKVNE SMKNYKVHEM ANYLINFLVE
     DVSRFYIRLI RKRAWIEANT QDKIAMYYIL YFILKQWIIL ASTIIPFISE KIYKSFVVNP
     KESVSMESSI NYDERFIDNE LERAFEVARE INEASLNARA KAGIKLRWPL AKVYIFVEDE
     DTLAKVNRIK DVLLSLLNAK DIEISKIEGF KSFSKYKVEP NRSIIGKEYK SMSPKILDYI
     RNNSDIIAID ILNKKQHVAR IDNVDVILNT SHVIISEETI EGYVSSKFAQ GIVVISKEIS
     ESEEEEGLVR DIIRRIQFMR KQLKLNVVDY IEISIKAPEE RVKTIQKWEE FIKSETRGNK
     VILGDPKGDI VMDWDIEGES YIIGIKKST
//