ID   SYI_METKA               Reviewed;        1080 AA.
AC   Q8TWY2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 123.
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=MK0899;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales;
OC   Methanopyraceae; Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(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; 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; AE009439; AAM02112.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TWY2; -.
DR   SMR; Q8TWY2; -.
DR   STRING; 190192.MK0899; -.
DR   PaxDb; 190192-MK0899; -.
DR   EnsemblBacteria; AAM02112; AAM02112; MK0899.
DR   KEGG; mka:MK0899; -.
DR   PATRIC; fig|190192.8.peg.941; -.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   InParanoid; Q8TWY2; -.
DR   OrthoDB; 30823at2157; -.
DR   Proteomes; UP000001826; 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   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42765; 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; 2.
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; Reference proteome; Zinc.
FT   CHAIN           1..1080
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098582"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           628..632
FT                   /note="'KMSKS' region"
FT   BINDING         631
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1080 AA;  126028 MW;  0024CBCD26D75BC0 CRC64;
     MGAGEMAEAL GEELEREIQR RWEEMDLLSK VLEKNRDGPL FYFLDGPPYA SGSIHLGTAW
     NKIIKDAVNR YKLMRGYRVR LQPGWDCHGL PIEVKVEQEV LSDEIECKKD IEEKVGVDKF
     VEKCKEFALK HVEIMTEQFK RLGVLMDWDN PYMTLDNEYI EGAWYTLKRA HERGLLDRDV
     RIVNWCPRCE TALADHEVEY KEVEDPSIFV IFPIEDDSDA EVDLPENSAL LIWTTTPWTL
     PANLAVAVHP EEEYVLARAE VDGEEWHLIV ADKLKVVLSV VTDSYEIVDS FPGEALEGLR
     YRPPLWEEVP KLRELHEEDD RVHRVYTAEW VTMEEGTGCV HSAPGHGEED FELGREVGLP
     PHCPVAEDGT FTEDGGKYEG LYVRDANEKI VEDLREKGLL AHEDTVEHRY GHCWRCKTPI
     IYRATEQWFL KVTEVKDEML EWIERVEWIP EWAGHSRFKS WVENARDWCI SRQRYWGIPL
     PVWECEECGH LEVIGSLSEL EAKAVSLPPG EPDLHRPWVD EVVLKCPECG SYMRRVPDVL
     DVWVDSGVAA WASLGYPRRE DEFERWFLKE GRCDPDDPEA GADFITEGHD QTRGWFYSQL
     GCGVVTFDTC PYRTVLMHGF TLDEEGRKMS KSLGNVVDPM DVVEKYGADT LRWYVLRSNA
     PWRDMHFSWQ DVRDTHRALN VLWNAYRFTK MYSELDEFDP EEHPLEDLEE HLKPEDRWLL
     SRINSLVEEV TDAFERYHVH EAARALYRFV TEDLSRWYIR LVRERVWLEG DDPEKLAVYA
     VLHYTFDRLV RLLAPIVPHV AERIYLDYVR AGDDPESVHL TDWPEVDDRW VDEGLEKAME
     LVRKAAEAAL SVRQRAGVKT RWPLRRLFVE VEDPKRLEDL KDVLARVANV KEVELGEEFP
     EKVPVAEPRP DKIGPEFRSL AGRVIEHVKD RAEEVARSIL KDGEYRTELD GEDVVLTEEH
     VKVTEDLPEG WEAEEFEGGR VYVFVELDEE LKSEAWAREV VRRVQEMRKE LDLNLEERIR
     VWIETDEEIA EAVEEHSEYV RGETRADELH VNEGWPEEVD LEREWEVEDR TIRIAVVVSG
//