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 27-MAR-2024, entry version 114.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 OrthoDB; 30823at2157; -.
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 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; 1.
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..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
//
