ID   SYI_METTP               Reviewed;        1049 AA.
AC   A0B7P3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Mthe_0929;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000477; ABK14717.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B7P3; -.
DR   SMR; A0B7P3; -.
DR   STRING; 349307.Mthe_0929; -.
DR   EnsemblBacteria; ABK14717; ABK14717; Mthe_0929.
DR   KEGG; mtp:Mthe_0929; -.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   OMA; HLGTAWN; -.
DR   Proteomes; UP000000674; 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   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 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   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.
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..1049
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000022157"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           596..600
FT                   /note="'KMSKS' region"
FT   BINDING         599
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1049 AA;  121605 MW;  F491CBA9FA700B1E CRC64;
     MIVEVPGQYN PKNVEDEVRE FWHREDTYHK VRRLRSGGRR FFFVDGPPYT TGRIHLGTAW
     NKVIKDSILR YMSMRGYDLK DRAGWDMHGL PIEVKVEEHL GFRSKRDIES YGVDRFIEQC
     KSFALRQKDE MTEQFKSLGV WLDWDNPYMT LKNEYIEAAW WTLKRAHERG LLERGLRVVN
     WCPRCQTAIA DSEVEYWDES DPSIYVKFPV EGEDNTYIVI WTTTPWTIPA NVAVAVHKDF
     MYSKVRAWRR DGTYEILIMA TDLIENVLKQ GRYVDYEILE SMRGEDLLSL TYKNPLQDLV
     PAQRDIVHRV HLADFVTAEN TGIVHIAPGH GLEDYELGLE KRLPIFCPVG EDGRYTSEAG
     KKYEGKYVRD ANPEVVEDLM ERGALLASGE LVHRYGHCWR CKTPIIFIAT RQWFIGISEL
     RDQMLKEIER VSWYPDWAGS ARFKDWISNA RDWCISRQRY WGIPLPIWIC RSCGAMDVIG
     TAAELEARAG RPVEDLHRPA VDDVRLRCSC GGAMERVPDV FDVWFDSAVA SWATLNFPRD
     EEEFRVWWPA DFITEGHDQT RGWFYSQLGA SMVAFGRAPY KSVLMHGFTL DEQGRKMSKS
     IGNVVHPEDV VERYGADTLR FYVLSSNAPW EDLHFSWEGA MNVNRMLNIL WNAYRFPLPY
     MVLDRFDISK ADTSKYDLRP EDRWIISRVN SLAKEIEENM SGYMLHRATR SLQEFVLEDL
     SRWYIQLVRP RTWIETEDPD KLAAYATLYN VMSTLVKLMA PFTPFLAESI YQNLVRGLDP
     SAPESVHMCD WPGYREDLID KGLEESMSYV REISEAAANA RQKGGRKLRW PVSRIIIASD
     EQLDLRDLLH VLRTQTNSKE VIILPPGEKP EMNLEISVVQ KKIGPVFKGE SRDVVEALTS
     MNPKEVKRII ESGEPLEWKG RSYMITEEMV EFREIPPANL IPAEFSKGTV YVDVSLTDEL
     RAEGYAREII RRIQDMRKDL DLKVDEMIRV SVALNSNEVV DLVSGWRDYI SSEVRATLLR
     IGNDLDLEGE LTKDWEVDGV KIRVSVARA