ID   SYI_METAR               Reviewed;        1104 AA.
AC   Q0W720;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=UNCMA_23590;
GN   ORFNames=RCIX379;
OS   Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the rice
RT   rhizosphere.";
RL   Science 313:370-372(2006).
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; AM114193; CAJ35823.1; -; Genomic_DNA.
DR   RefSeq; WP_012036678.1; NC_009464.1.
DR   AlphaFoldDB; Q0W720; -.
DR   SMR; Q0W720; -.
DR   STRING; 351160.RCIX379; -.
DR   EnsemblBacteria; CAJ35823; CAJ35823; RCIX379.
DR   GeneID; 5145666; -.
DR   KEGG; rci:RCIX379; -.
DR   PATRIC; fig|351160.9.peg.2409; -.
DR   eggNOG; arCOG00807; Archaea.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 4914at2157; -.
DR   Proteomes; UP000000663; 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; 2.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; SSF47323; 2.
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..1104
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000022161"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           644..648
FT                   /note="'KMSKS' region"
FT   BINDING         647
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1104 AA;  125895 MW;  5958154F4B06387E CRC64;
     MIQEEKEQYS SKSLEAGVDE LWRASDAYAL TRKKRLGSKR FFFVDGPPYT TGRIHLGTAW
     NKIIKDSVLR YRSMNGYDLI DRPGWDMHGL PIEVKVESIL GFKTKKDIEE FGVARFTEEC
     KKFAIGNMHE MTSQFKKLGV WMNWDDPYMT LKNEYIEAAW WTIKQAHEKH LLERGLRNVN
     WCPRCETAIA DSEVEYADRK DDSIYVKFPL KNEEGFLVIW TTTPWTIPAN MAVAANKDFT
     YAMVYALPAA VLEEAAMQAG LDHTTLVEHH SDGRPKPMRY SDKVAKMKEA IGEEKVKELY
     EKHGEKLIIA RDLVDGVLKM GRYADYQVLK TMTGEELKGT EYVHPLADLI PCQKETEHKV
     YLADFVVGEN TGMVHIAPGH GFDDFELGLK EGIRAYCPVK ANGHYDDSVG AYAGMEIREA
     NPKIMEDLRQ RNLLLGATTI EHRYGHCWRC KTPIIFLTTD QWFIAVSKMK EDMLAEVKRV
     NWYPDWAGSA RFYDWVNGAR DWCVSRQRYW GIPIPIWKCE KCGSLDVIGT KEELERKVGR
     EVPDLHRPFV DEVRLECECG GSMRRVEDIF DVWFDSAVAS WATLHFPGRK DLMDWWPADF
     IVEGHDQTRG WFYSQLGAGM VGFGKAPYNG VCMHGFTLDE TGKKMSKSLG NVVAPEDVVE
     KLGADTLRLY VLSQNAPWED LSFSWEECGN INRAINIFWN VYRFPLPYMV LDKFDPAKVT
     LESVKGSLRV EDRWILSKLQ AVIKDVDTYM ATYELHRATR SIISFILEDL SRWYVQLARE
     RTWVEADDPD KLAAYRVLYD TLVTTVKLIA PFTPYIAERM YQNLVRNVSA EAPVSVHMCD
     WPVVDSSLLD EQLNRDMDIA RKIVEASSNA RQKAKRKLRW PVQKIVVAAE NPDVVTAVKD
     LSGVIGEQTN SKEVVVLAPG EANTELGVEV VPNPKLIGPI FKAVAGKVTA ALKEADGRAV
     KKAIEEEKKY IVEIPEGSFD ILLDMVSFRD VIPESLAMAD FPGGKVYVDV TLSKELEAEG
     YTRELIRRIQ DMRKEMNLNV EDRIKVEVYV GDEKVLDLVK SMKDYAAGEV RADTLDLKTE
     KPAAGFVKDW DVEGIPMTIG LEKI