ID   SYI_METMP               Reviewed;        1034 AA.
AC   Q6LX78;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=MMP1474;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF31030.1; -; Genomic_DNA.
DR   RefSeq; WP_011171418.1; NC_005791.1.
DR   AlphaFoldDB; Q6LX78; -.
DR   SMR; Q6LX78; -.
DR   STRING; 267377.MMP1474; -.
DR   EnsemblBacteria; CAF31030; CAF31030; MMP1474.
DR   GeneID; 2761573; -.
DR   KEGG; mmp:MMP1474; -.
DR   PATRIC; fig|267377.15.peg.1510; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 4914at2157; -.
DR   BioCyc; MMAR267377:MMP_RS07585-MON; -.
DR   Proteomes; UP000000590; 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   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; 1.
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..1034
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098581"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           598..602
FT                   /note="'KMSKS' region"
FT   BINDING         601
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1034 AA;  119910 MW;  A9C573A4C0E3ECB8 CRC64;
     MKQVKSVNFR ELDKKVKEYW KKENTYKKVK ALNEHGPEYY FVDGPPYCSG AIHLGTAWNK
     IIKDTVLRFK RIQGYNVLDK AGWDMHGLPI EVKVENEFNI GSKKDIETKI GTQEFINKCK
     EFALNHLGHM QGQFENLGVW LDFENAYMPI KRDYMEMGWW TLKKAHEKEL LTKDLRSGYW
     CPRCETSLAE HEVRGEYKEV LDPSVYVKFK LEKSDEYITI WTTTPWTLPS NMLVCVNPEF
     DYAYVNVEFE NGTAETWIIA EKLVNDVMKK AEKNNDISKF SISKVVKGDS LIGLKYIHPL
     LEENEKQQEF AKIENVHTIV PGDHVTLEGG TGLVHTAPGF GEDDFNIGKE HNIPVYAPID
     DNGKYTDSIW KGTFVKDMDE SVIETLISKN LLVNSGKVKH TYPHCWRCKT PLLFRATEQW
     FLSISKIKDS IIEQGKTVDW VPDWVKTRYV NGVSFVGDWN ISRQRYWGIP LPIWICEECG
     NYEVIGSVDE LKERANEKDV DLSDIHKPAV DKITLTCSCG GKMKRTPDVL DVWYDSGLAP
     YASIGSKKLK KAQFITEGND QVTKWFYSQH ALSAVVFDDT SYEKCMMHGF TLDETGEKMS
     KSLGNIVSPD DVTEQYGADV LRFYLLSANK AWEDLRFSYS EMDETRSMLN TLWNSYAFSA
     NYMVLDDFVP NNEYFKHVKD EDAWILSRIN TVAKEAVEAL EKPHLHVYTW ALRDFILNDF
     SRWYIKLIRD RTWMEKNDVQ KLSAYQTLYY VIMKLISIMA PVTPHLSEEI YQNLKTEDMP
     ESIFMNKLTI ESEFINETLE KDTEIIREIV DSILKGRDKA KYTLRYPITK ITLPENIAET
     VEKYGYIIKE QGNVKEIELK EFEGNITVKP NFKELGKIFR SDVPKVVAAI NSVAPNELKE
     KLKSGNFEVS EYEIKPEYVE FRVEIPENIV GVEFSKGNVY INIEMNDEVI KEGLVREVVR
     RIQSMRKDMD LDINEKINVK LEGIDFSSDY LSHIANEVRG NFVESLKSDY NQKWTIKTPN
     EETYDISIDI EKNK