ID   SYI_CLOPE               Reviewed;        1039 AA.
AC   Q8XHE4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 120.
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=CPE2541;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(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; 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; BA000016; BAB82247.1; -; Genomic_DNA.
DR   RefSeq; WP_011010955.1; NC_003366.1.
DR   AlphaFoldDB; Q8XHE4; -.
DR   SMR; Q8XHE4; -.
DR   STRING; 195102.gene:10491875; -.
DR   KEGG; cpe:CPE2541; -.
DR   HOGENOM; CLU_001493_1_1_9; -.
DR   Proteomes; UP000000818; 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..1039
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098534"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           593..597
FT                   /note="'KMSKS' region"
FT   BINDING         596
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1039 AA;  119383 MW;  9383D2B89FF0844D CRC64;
     MYKKVELPKG FVGVEKEVAD LWKEKNIIKK NFDMNQDGEY FTFYDGPPTA NGKPHVGHVL
     TRVMKDIIPR YKVMKGYKVI RKAGWDTHGL PVELEIEKKL GISGKPQIED YGVEKFVTEC
     KDSVFTYVSM WEKMTEQIGY WVDMENPYVT YHNPYIESVW WALKQMWDKK LLYKGYKTMP
     YCPRCGTSLS SHEVSQGYKD VKDLTAVAKF KVKGEDNKYF LAWTTTPWTL PSNVALCINK
     AYDYVEAKQA EGDEIFILAK ELAPKVLGEG FEIVREFKGE ELLGMEYEQL LPFVTPTEGK
     AFVVVHGDYV TLSDGTGIVH IAPAYGEDDN LIGKQNGLAF LNLVDLSGNF VEEVTPWAGK
     FVKKCDQQIV DYLKEQNKLF KAEKHTHSYP HCWRCDTPLL YYPKESWFVA MTTLRDKLLA
     NNEKINWYPD NIKNGRFGKF LENVIDWGIS RDRYWGTPLP IWECECGHRE CIGSIEELKT
     KGINVPEDIE LHKPYIDKVH LNCPHCNKEM KRTAEVIDCW FDSGSMPFAQ HHYPFENKEL
     FEANYPAQFI SEAVDQTRGW FYTLLAISTA IFDRNPFENC IVLGHVLDKK GLKMSKSKGN
     VVDPFEVLDS QGADATRWHF YTASAPWLPT RFSIEDVAET QRKFLSTLWN VYSFYVLYAE
     LDNFNPLDYK DFVSDNVMDK WIMSKLNTLV KDVDDHLNNY RITQAALEIE EFTDELSNWY
     VRRNRARYWS EELTDDKIGA YTTLYRVLVT LCKVAAPFVP FITEEIYQNL VVNLDENALE
     SIHLGAWPEV DEKAIDKKLE EKMDLAYKIV KLGRSARNGA NIKNRQPLSK MLLSTSELPE
     YYGDIIKDEL NIKEVELGAD LSKYVNFEIK PNLPVLGRAY GKLIPAIRKE IASRNQMELA
     QKIQNGGVEV ITVDGNEIEL NAENLLVTMQ GLEGFAFAGE GSVGVVLDTT ITDELREEGH
     VREIISKIQN MRKESGFEVA DKITLYVAEN DMLLDVIKKF EDVIKKETLT EEIVYNGNAD
     YSEAKVNGEI LKMAVSKRA
//