ID   SYI_METAC               Reviewed;        1058 AA.
AC   Q8TN62;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, 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=MA_2431;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(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; AE010299; AAM05817.1; -; Genomic_DNA.
DR   RefSeq; WP_011022402.1; NC_003552.1.
DR   AlphaFoldDB; Q8TN62; -.
DR   SMR; Q8TN62; -.
DR   STRING; 188937.MA_2431; -.
DR   EnsemblBacteria; AAM05817; AAM05817; MA_2431.
DR   GeneID; 1474320; -.
DR   KEGG; mac:MA_2431; -.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   InParanoid; Q8TN62; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 4914at2157; -.
DR   PhylomeDB; Q8TN62; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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_0000098583"
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;  120217 MW;  3940FED68C23AEA3 CRC64;
     MIKEITAKYN AEQIEKKVTQ FWEDSDAYRK TRERRKTGKR LFFVDGPPYT TGHIHLGTAW
     NKIIKDTILR YYSMNNRYIL ERPGWDMHGL PIEVRVEGVL GFKSKKDIES FGVENFIEKC
     KEFAITQKQA MTEQFQRLGV WMQWPEPYMT LKDDYIEAAW WTLKQAHEKD LLEVGKRSVN
     WCPRCETAIA DSEVEYSERT DPSIYVKFKV KGEENTFIVI WTTTPWTIPA NVAVAVHPAY
     EYSKFRAIRQ DGSEEILIAA TELIKNVLKQ GRYADFKVLE TMLGEELTKL EYESPVGDLV
     PIQNEIKHGV YLADFVTVEN TGCVHIAPGH GMDDFNLGVK HKLPILCPVG SNGAYTEEAG
     EYAGKNVREA NPIVIEDLKA RNRLLAEGTV THRYGHCWRC KTPIIYLATE QWFLKITEIK
     EKMLEEIDAV DWYPDWAGSA RFRTWVEGAR DWCISRQRYW GIPLPVWKCK KCGKLEVIGT
     KAELLEKAGL SGDIELHRPY VDRVTVPCEC GGEKKRVEDV FDVWFDSAVA SWATLKFPQT
     HDQFDEWWPA DFVTEGHDQT RGWFYSQLGA SMVGFGRAPY KSVLMHGFTL DAGGKKMSKS
     LGNVVSPLDI IDRLGADTLR AYVLSSSAPW EDLKYNLEEV ETVHRSINIL WNVFRFPLPY
     MALDNFDPMQ VSLDSVKDAL REEDRWILSR AQSVIKAVNE AMSGYLLHKA VREILEFALE
     DLSRWYIQLI RPRTWTEADD PDKLAAYCVL YEVYVTITKL ISPFMPYLAE EMYQNLIRNV
     DPNAPESVHM CDWPKVNDTY LDPELEVAMD TVRSIVEAAS NARQKAGRKL RWPVSRIIVS
     PESEAAAKAV NRLGSVLMDQ TNSKAIVLTG VGKSWDELGL EVIPDPGKIG PVFKKDAGRV
     IPALQKVEGF TLKKAFAETG EFELTLADGT TVPVTSGMAN FKETLPEGTA SAESDAGLVY
     VDANLTPELE AEGYAREVIR RLQDMRKELD LVVDENIRVS VRIEAEKVLA LVETLKDLIA
     EEVRADVFDL GSSIEVSGTL VKDWDVEGTA MKMGIAKK