ID   SYI_METMJ               Reviewed;        1059 AA.
AC   A3CSI6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Memar_0403;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000562; ABN56336.1; -; Genomic_DNA.
DR   RefSeq; WP_011843246.1; NC_009051.1.
DR   AlphaFoldDB; A3CSI6; -.
DR   SMR; A3CSI6; -.
DR   STRING; 368407.Memar_0403; -.
DR   EnsemblBacteria; ABN56336; ABN56336; Memar_0403.
DR   GeneID; 4847697; -.
DR   KEGG; mem:Memar_0403; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 4914at2157; -.
DR   Proteomes; UP000002146; 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; Zinc.
FT   CHAIN           1..1059
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000022156"
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   1059 AA;  120495 MW;  9C554469148FCFD1 CRC64;
     MKEVTGSYNP RELEAGVQDT WKRENTYARV QEVRKDGKAF FFVDGPPYTT GHIHLGTAWN
     KIIKDTILRY HRMGGRNIIE RAGYDMHGLP IEVKVEHQLG FTSKKDIEDY GIAAFIEQCR
     TFAVTHMEIM SEQFRQLGIW LDFDDPYQTI KAEYIESAWW AVQRAEERGL LERGHRVVNW
     CPRCETAIAD SEVEYWDETD PSIFVKFPVT GRENEYLVIW TTTPWTLPAN VAVAVSPAFT
     YARVAAKKDG SEEILWIADE LVESVLKMGR YQDYTVLERV NGSDLVGTEY ESPLAGQVPH
     QAEIRHRVVA ADYVALENTG LVHIAPGHGW DDYLIGIQEG LEAFCPVDAG GCFTREAGAF
     ADMYVRDAND LVIDALGDYL LARRTITHRY GHCWRCKTSI IYRATAQWFL KATEIREPML
     QEIAKVKWYP EWAGSARFHD FVRDSRDWCI SRQRYWGIPI PIWQCEQCGE RTVIGTIAEL
     EERSGARVPD PHRPYVDEVV IPCSCGGEMH RVADIFDVWF DSAVASWATL GFPREREAFD
     RLWPADFITE GQDQTRGWFY SQLGASTVAF GRAPYKSVLM HGFALDADGR KMSKSFGNVV
     TPEEVMNQFG VDVLRFYVLW ANAPWDDLKF NWDSVKTIHR TLNILWNVYR FPLPYMVLDS
     FEPAAGDGGL WDGSFVRGNI NDMPEEDRWI ISRVNSLART TAGDMQEYHL HRVTRALAAF
     ILEDLSRWYV QLVRPRMWLE EDSPEKRYAY ETVYYVMRRL VALLAPFTPH IAEEIYGNLR
     LAGDPESVHM LDWPEADDLL IAPDLESAME VVRSFDDAVA TARQNGRRKL RWPVAETVVV
     TGSDGVKTAL EDLNDLALNR ANSRTVRVVT GRWDRILWQA EPVMRAIGPE FGKEGPKVKA
     LIEGADGTAL KAAIERDGKA ELGGYEIAER HVTFAEALPE GVFAAPMKDA TVYVDVTLTP
     ALEAEGYARE VIRRIQEMRR QLDLNVDDFI VAAVDVADDR VASLIAEEEW QKEIAGEVRA
     AALTVRRTDG ERPTETFALE KDWDVEGVQM QIGISRAGE