SYI_SULIA
ID SYI_SULIA Reviewed; 1049 AA.
AC C3N5S5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=M1627_1468;
OS Sulfolobus islandicus (strain M.16.27).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=427318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.16.27;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(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; CP001401; ACP55350.1; -; Genomic_DNA.
DR AlphaFoldDB; C3N5S5; -.
DR SMR; C3N5S5; -.
DR EnsemblBacteria; ACP55350; ACP55350; M1627_1468.
DR KEGG; sim:M1627_1468; -.
DR HOGENOM; CLU_001493_1_1_2; -.
DR OMA; HLGTAWN; -.
DR Proteomes; UP000002307; 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; 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; Zinc.
FT CHAIN 1..1049
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_1000216258"
FT MOTIF 48..59
FT /note="'HIGH' region"
FT MOTIF 597..601
FT /note="'KMSKS' region"
FT BINDING 600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1049 AA; 121984 MW; 6E9C7F840E1C9E40 CRC64;
MKPLTGNYDP KKIEDEIISF WEENKIYNKL RDIVSKRREK FLFIDGPPYP SSPTPHIGTI
WNKVIKDCIL RYERLLGKKV HDQPGYDTHG LPIEVATERL LGILNKQEII DKIGVENFIN
KCKEFALSNA TKMTQNFKDV GVFMDWERPY YTLDPSYISS SWSVIKKAYE KGMLDKGTAV
LHWCPRCETT LSDYEVSEYR DLEDPSIYVK FKIKGEENRY LLIWTTTPWT IPSNVFVMVN
KDYDYADVEV NGEVLVLAKD RIEAVMKEAS ITNYKVLRTY KGSELIGVKY KHPLRDFVSA
QTKLDDFHQV VDAGNVVTLT DGTGLVHAAT GHGEEDFLIG QKYGFPVVMF VNDRGEFTEE
GGKYKGLKVR DASKVIINDL KSKNALFFEG KIVHRYPVCW RCKTPLVLRA IDQWFIRVTK
IKDEMLKEIE NVNWIPDWGK SRISNMVKEL RDWVISRQRF WGTPLPIWIC EKCNNVIVVG
SREDLESIAI DSVPNDLHRP WIDNVRVKCN KCGGVAKRIA DVADVWFDSG VAFFASLGKD
WQEKWKELGP VDLVLEGHDQ LRGWFFSLLR SGLILLDKAP YVSVLVHGFM LDEQGREMHK
SLGNYVEPSV VIQRYGRDIL RLWLLRNTTW EDARFSWRAL ELTKRDLQII WNTYVFASMY
MNLDNFEPVK YTLDDVIKYA KIEDLWILSR FNSMLKKVNE SMKNYKVHEM ANYLINFLVE
DVSRFYIRLI RKRAWIEANT QDKIAMYYIL YFILKQWIIL ASTIIPFISE KIYKSFVVNP
KESVSMESSI NYDERFIDNE LERAFEVARE INEASLNARA KAGIKLRWPL AKVYIFVEDE
DTLAKVNRIK DVLLSLLNAK DIEISKIEGF KSFSKYKVEP NRSIIGKEYK SMSPKILDYI
RNNSDIIAID ILNKKQHVAR IDNVDVILNT SHVIISEETI EGYVSSKFAQ GIVVISKEIS
ESEEEEGLVR DIIRRIQFMR KQLKLNVVDY IEISIKAPEE RVKTIQKWEE FIKSETRGNK
VILGDPKGDI VMDWDIEGES YIIGIKKST
