ID   SYI_CLOTE               Reviewed;        1036 AA.
AC   Q899C3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   27-MAR-2024, 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};
GN   OrderedLocusNames=CTC_00261;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO34906.1; -; Genomic_DNA.
DR   RefSeq; WP_035110918.1; NC_004557.1.
DR   AlphaFoldDB; Q899C3; -.
DR   SMR; Q899C3; -.
DR   STRING; 212717.CTC_00261; -.
DR   GeneID; 24253432; -.
DR   KEGG; ctc:CTC_00261; -.
DR   HOGENOM; CLU_001493_1_1_9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001412; 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   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; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR42780; 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; Reference proteome; Zinc.
FT   CHAIN           1..1036
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098535"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           590..594
FT                   /note="'KMSKS' region"
FT   BINDING         593
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1036 AA;  120322 MW;  53261B634ADDD476 CRC64;
     MYKKIDGSKS FVQMEREVLD FWNKNNIVDK SFALNEEGEY FTFYDGPPTA NGKPHVGHVL
     TRVIKDLIPR YKVMKGYKVL RKAGWDTHGL PVELEIEKKL GISGKEEIEK FGVEEFIKEC
     KDSVFTYSSM WKDMSEKLAF WVDMENPYVT YHNDYIESVW WALKQLWNKE LLYKGHKVIP
     YCPRCGTALS SHEVAQGYKD VKEATAFVKF KVKGEENKYI LAWTTTPWTL PSNVALAINK
     NFDYVEVKNN DEVLILAKEL VDSVIDGEYE IIKEFKGEDI LGLQYEQLLP FYTPEEEAFR
     VIHGDFVTLS DGTGIVHTAP AYGEDDNIVC KKHGLPMINL VDKEGKFIDC VEPWKGMPVK
     KADSKIIEYM DEKGILYKSE KFTHSYPHCW RCDTALLYYP TDSWFVRMTS LRDKLLENNN
     KVNWYPDNIR TGRFGKFLEN VIDWGISRDR YWGTPLPIWE CECGHRECIG SISELKEKGI
     DVPEDIELHK PYIDKVKLKC SKCGKEMKRT REVIDCWFDS GSMPFAQHHY PFENKEVFEK
     TFPAQFISEA VDQTRGWFYT LTAISTAIFD TNPFENCIVL GHVLDKHGLK MSKSKGNVVD
     PFDVLDSAGA DASRWHFYTA SAPWLPTRFS PEDVEETQRK FLSTLWNVYS FYVLYADIDK
     FNPLEYKDFV SENVMDKWIV SKLNSLIKDV EDHMDSYRIT QAALAIEDFV DELSNWYVRR
     NRSRFWSEEL REDKIGAYVT LYKVLTTVSL IAAPFVPFIT EEIYNNLVRG LDKNALESIH
     LCNWPKYDEN LIQKELEREM DEAYKIVKLG RSARNSVNIK NRQPLSSMLV SIKTLPEYYG
     RIIKDELNIK DIIFGADLSS YVEFNIKPNL PVLGKAYGRY IPQIRKEITS MDQMKLAQKI
     KQGEKVIINI DGNEIELNEE NLLVTMKGLE GFAFAGEGNI GVVLNTTITD ELKEEGQLRE
     ILSKIQNMRK EKEFEVADRI KLYVSGNRML ESVVEKFEDI IRKETIAEEV IYNEEREYVD
     CKINGEDFKI EVEAIK
//