ID   SYI_METBF               Reviewed;        1058 AA.
AC   Q465G4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 128.
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};
GN   OrderedLocusNames=Mbar_A3613;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000099; AAZ72478.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q465G4; -.
DR   SMR; Q465G4; -.
DR   STRING; 269797.Mbar_A3613; -.
DR   PaxDb; 269797-Mbar_A3613; -.
DR   KEGG; mba:Mbar_A3613; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   OrthoDB; 30823at2157; -.
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; 3.30.720.200; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   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; Zinc.
FT   CHAIN           1..1058
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000022152"
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;  120510 MW;  81BE7252A232D33A CRC64;
     MIKEITAKYN AEQIEKKITQ LWKDSDAYRK TREHRKTGKR LFFVDGPPYT TGHIHLGTAW
     NKIIKDSILR YYSMNNRNIL ERPGWDMHGL PIEVKVEGVL GFKSKKDIES FGVENFIEKC
     KEFAINQKQE MTEQFQRLGV WMQWEAPYMT LKDDYIEAAW WTLKQASEKN LLDVGKRSVN
     WCPRCETAIA DSEVEYAERT DPSIYVKFKI KGEENTFIVI WTTTPWTIPA NVAVAVHPGF
     EYSKFRAIRQ DGSDEILIAA TDLIENVLRQ GRYVDYEVLE TMLGEDLTKL EYESPVGDLV
     PVQNEIKHGI YLADYVTAEN TGCVHIAPGH GMDDFNVGVK YNLPILCPVG PNGAYTEEAG
     EYAGKNVREA NPIVIEDLRK RNRLLAEGTV THRYGHCWRC KTPIIYLATE QWFLKVTDIK
     DKMLEAIDAV DWYPEWAGSA RFRTWVEGAR DWCISRQRYW GMPIPVWKCK KCGKLEVIGT
     KAELLEKSGA GSDVELHRPY VDKLTIPCEC GGEKKRVEDV FDVWFDSAVA SWATLKFPQT
     REQFDEWWPA DFITEGHDQT RGWFYSQLGA SMVGFGRAPY KSVLMHGFTL DAGGKKMSKS
     LGNVVSPIDV IDKYGADTLR AYVLSSSAPW DDLKFNQEEV ENVHRSINIL WNVFRFPLPY
     MALDNFDPLK VSLDSVKDAL REEDRWILSR IQSVVKAVDE AMSGYFLHKA VREILEFTLE
     DLSRWYIQLI RPRTWTEADD PDKLAAYRVL YEVYVTLTKL ISPFMPYLAE EMYQNLIRNV
     DPNALESVHM CDWPKVNEAY LDPELEAAMS TARSIVEAAS NARQKAGRKL RWPVSRIVVS
     PESEDAAKAV ERLRSVLMDQ TNSKAIVLTP VGESWDELGL EVIPDPSKIG PVFKKDAGKV
     IPALQKVDGF ALKKAFAEAG EFELSLADRT TVTVTPGMAN FKETLPEGTA SAESDAGLVY
     VDANLTPELE AEGYAREVIR RLQDMRKELD LVVDENIRVS VRIEDERVLR LVETLKDLIA
     EEVRAEILNL GSDIDVSGAL VKDWDVEGIA MKMGISKK
//