ID   SYI_METMA               Reviewed;        1058 AA.
AC   Q8PSV9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 129.
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=MM_2967;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(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;
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; AE008384; AAM32663.1; -; Genomic_DNA.
DR   RefSeq; WP_011034868.1; NC_003901.1.
DR   AlphaFoldDB; Q8PSV9; -.
DR   SMR; Q8PSV9; -.
DR   STRING; 192952.MM_2967; -.
DR   EnsemblBacteria; AAM32663; AAM32663; MM_2967.
DR   GeneID; 1481309; -.
DR   KEGG; mma:MM_2967; -.
DR   PATRIC; fig|192952.21.peg.3444; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   OMA; HLGTAWN; -.
DR   Proteomes; UP000000595; 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..1058
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098584"
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   1058 AA;  120411 MW;  8BA5C0DE0FDCE4F3 CRC64;
     MIKEITAKYD AEQIEKKVTQ FWEDSDAYRK TREHRKSGKR LFFVDGPPYT TGHIHLGTAW
     NKIIKDSILR YYSMNNRYIL ERPGWDMHGL PIEVKVEGVL GFKSKKDIES FGVENFIEKC
     KEFAIKQKQA MTEQFQRLGV WLQWPDPYMT LKDEYIEAAW WTLKQASEKD LLEVGKRSVN
     WCPRCETAIA DSEVEYSERT DPSIYVKFRV KGEENTFIVI WTTTPWTIPA NVAVAVHPAY
     EYSKFRAIRQ DGSEEILIAA TELIKNVLKQ GRYTDFEVLE TMLGEELTKL EYESPVGDLV
     PVQNEIKHGV YLADFVTVEN TGCVHIAPGH GMDDFNLGAK HKLPILCPVG SNGSYTEEAG
     EYAGKNVKEA NPIVIEDLKA RNRLLAEGTV THRYGHCWRC KTPIIYLATE QWFLKVTEIK
     EKMLEEIDAV DWYPDWAGSA RFRTWVEGAR DWCISRQRYW GIPIPVWKCK KCGKLEVIGT
     KAELLEKAGL NGDIELHRPY VDRVTVPCEC GGEKKRVEDV FDVWFDSAVA SWATLKFPQT
     RDQFDEWWPA DFITEGHDQT RGWFYSQLGA SMVGFGRAPY KSVLMHGFTL DAGGKKMSKS
     LGNVISPLDI IGRFGADTLR AYVLSSSAPW DDLKFNLEEV ETIHRSINIL WNVFRFPLPY
     MALDNFDPMQ VSLDSVRDAL REEDRWILSR AQSVVKSVDE AMSGYLLHKA VREILDFTLE
     DLSRWYIQLI RPRTWTEADD PDKLAAYCVL YEVYVTITKL ISPFMPYLAE EMYQNLIRNV
     DPKAPESVHM CDWPKVNEAY LDTKLEEAMN TARSIVEAAS NARQKAGRKL RWPISRIVVS
     PESEDAARAV ERLRSVLMDQ TNSKDIVLTG VGKSWDELGL EVIPDPGKIG PVFKRDAGKV
     VPALQKVDGF ALKKAFAEAG EFELTLADGS TVKVTPEMAN FKETLPEGTA SAESDAGPVY
     VDANLTPELE AEGYAREVIR RLQDMRKELD LVVDENIQVS VRIEDERVLK LVETLKGLIA
     EEVRADVFDI GSGVNVSGDL VKDWDVEGIA MKMGIAKK