ID   SYI_METHJ               Reviewed;        1062 AA.
AC   Q2FPJ4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=Mhun_0606;
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD40364.1; -; Genomic_DNA.
DR   RefSeq; WP_011447649.1; NC_007796.1.
DR   AlphaFoldDB; Q2FPJ4; -.
DR   SMR; Q2FPJ4; -.
DR   STRING; 323259.Mhun_0606; -.
DR   PRIDE; Q2FPJ4; -.
DR   EnsemblBacteria; ABD40364; ABD40364; Mhun_0606.
DR   GeneID; 3924432; -.
DR   KEGG; mhu:Mhun_0606; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 4914at2157; -.
DR   Proteomes; UP000001941; 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; 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..1062
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000022154"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           591..595
FT                   /note="'KMSKS' region"
FT   BINDING         594
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1062 AA;  121693 MW;  55CE0BEDE48AC9EB CRC64;
     MQEVTSSFTP RVIEASVQKF WTQEDIYARV QEQNRDGKTW FFVDGPPYTT GHIHLGTAWN
     KILKDSILRY KRMHGLHVID RAGYDMHGLP IEVRVEHELG FENKKDIEAF GIGAFIERCK
     QFALSHKDIM SEQFKSLGVW MNFDDPYQTI MPEYIEAAWW TLKQADEKGL LDRGHRVVNW
     CPRCETAIAD SEVEYWDEQD PSIFVKFPIH GLMNEYLVIW TTTPWTLPAN VAVAVDKDFI
     YARVEAIKEG KKEILWIAKD LVEPVLKRGK YQDYSILSEK TGEELAGTTY DSPLADLIPR
     QKEIVHTVVT AGFVEMDNTG MVHIAPGHGW DDYLLGVEKG LDVFCPVDGA GYYTDEGGIY
     AGQFVRDANE KILSDLGSHL LGRQKITHRY GHCWRCKTPI IYRATEQWFI SVPKMKEKML
     SEIKATSWYP DWAGSARFYD FVSDARDWCI SRQRYWGIPI PVWQCSSCSA HRVFGTVAEL
     NAAAGSNLTD PHRPYVDEIT VPCSCGGTMK RVEDIFDVWF DSAMASWATL GFPRNDALFH
     EMWPADFITE GQDQTRGWFY SQLGASTIAF NRSPYKSVLM HGFALDADGR KMSKSLGNVV
     TPEEVVQKFG VDVLRLYILS SNAPWEDLKF NWDGVSTVNR TMNILWNVYR FPLPYMILDG
     FSPAQTSDGK YDDEYIVRSY REMPEIDRWI ISRINTIARS VSADMDEYQL HRVTRLLMNF
     ILEDLSRWYV QIVRPRMWLE EDSPDKKFAY ETITYCLRTL CRLLAPFTPH ITEAMYENLR
     LPEDPVSVHM LKWPAGDIRL IDENLERRMD VVRKFDEAVA NARQAGKRKL RWPVQNVIVV
     TSSESVIEAF RSMEDLAKDR ANTRNIEVIQ GSWERMRFNA EPVMKKIGPS FGKKGPVVKG
     LIEAADGSAL RKQLEESGSV TLSDGSEEFV LTAEHMTFSQ HLPEGIFGAE MTDASVYVDT
     TLTEDLEAEG YSREIIRRLQ EMRKQLDLNV EDNIVIDAVI EDVHLRELLS ASWLDLIKQE
     VRGKTLKIHD SVGGRDGSVL FQLDRDWDIE GVNVTLGISL AG