SYI_THEMA
ID SYI_THEMA Reviewed; 919 AA.
AC P46213;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02002};
DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02002};
DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02002};
GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02002}; OrderedLocusNames=TM_1361;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-599.
RX PubMed=7708661; DOI=10.1073/pnas.92.7.2441;
RA Brown J.R., Doolittle W.F.;
RT "Root of the universal tree of life based on ancient aminoacyl-tRNA
RT synthetase gene duplications.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:2441-2445(1995).
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_02002}.
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_02002};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02002};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_02002};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02002}.
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_02002}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}.
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DR EMBL; AE000512; AAD36431.1; -; Genomic_DNA.
DR EMBL; L37104; AAC41448.1; -; Genomic_DNA.
DR PIR; B72263; B72263.
DR RefSeq; NP_229162.1; NC_000853.1.
DR RefSeq; WP_004081557.1; NZ_CP011107.1.
DR AlphaFoldDB; P46213; -.
DR SMR; P46213; -.
DR STRING; 243274.THEMA_07535; -.
DR PRIDE; P46213; -.
DR EnsemblBacteria; AAD36431; AAD36431; TM_1361.
DR KEGG; tma:TM1361; -.
DR eggNOG; COG0060; Bacteria.
DR InParanoid; P46213; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000008183; 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; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023585; Ile-tRNA-ligase_type1.
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 InterPro; IPR010663; Znf_FPG/IleRS.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF06827; zf-FPG_IleRS; 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..919
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098494"
FT MOTIF 57..67
FT /note="'HIGH' region"
FT MOTIF 594..598
FT /note="'KMSKS' region"
FT BINDING 553
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 887
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 890
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 910
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 919 AA; 107156 MW; 40E4D0876010C385 CRC64;
MEYKNTLNLP KTSFPMKANL VNKEKVFLEE WEKMDLYNYV LEQRKGKPLF VLHDGPPYAN
GHIHIGTALN KILKDIVVKY KTMRGYRAPY VPGWDTHGLP IEHRVSQELG EKIKEMSPAE
IRKKCEEFAL RFVDIQREEF KRLGVRGDWE NPYITLKPDY EVKILDVFKT LVEQGNVYRS
LKPIYWCPRC RTALAEAEIE YHDHKSPSIY VKFRSKEDPN FFIVIWTTTP WTLPANVGIA
LHPDYEYSVV KVGEEKWVIA TDLLDAFSKE TGIDCSNVVE KIKGKDLEGK EFVHPIFDDR
TSRVILADYV SLETGTGCVH IAPGHGEEDY IYGHVQYGLP IVSPVDEEGR FTEEAGKYKG
MFIEDANEVI IEDLKRKGIL VHASSITHSY PHCWRCKGPV IFRATEQWFI SVDHNNLRQK
VLEEIDKVKW IPEWGRNRIR SMVEERPDWC ISRQRVWGTP IPAVKCKECG EVVLDPKVIE
HFMKIVEKEG TNAWFEKEVE ELIPEDFVCP KCGKRSFEKM LDTLDVWIDS GASFEYITTK
REDHPFPLDM YLEGSDQHRG WFHSSIFLAV AKRGSAPYKE VLTHGFIKDE QGRKMSKSLG
NVVDPMEVVE KYGAEILRLW LASSDYFNDI KISMRIVEQQ TEVYRKIRNT FRFLLGNLED
FDPELDRVPH EKLLTIDRWA LGRLQEIIKR ATEYYDSYEF SKVYNLVVKY CTTELSSLYL
DVVKDRLYVE AKDSIYRRSA QTVMHEILIS LMKILAPIMT FTMEEVYSHL HEKDRKYKTV
QAEYWPEYRE EFIDRKLMED FEKLLSIRED VLKALEEKRQ QDVIGHSLDA EVVLVPKNDT
IKALLEKYRD ILEELFIVSK VSLSDASGEL KGELVEVTVK HAEGEKCQRC WKYTTEISAS
EDFPGVCPRC LAVLKGERK
