SYI_KOSOT
ID SYI_KOSOT Reviewed; 921 AA.
AC C5CHA1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Kole_0011;
OS Kosmotoga olearia (strain ATCC BAA-1733 / DSM 21960 / TBF 19.5.1).
OC Bacteria; Thermotogae; Kosmotogales; Kosmotogaceae; Kosmotoga.
OX NCBI_TaxID=521045;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Noll K.;
RT "Complete sequence of Thermotogales bacterium TBF 19.5.1.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001634; ACR78740.1; -; Genomic_DNA.
DR RefSeq; WP_012744528.1; NC_012785.1.
DR AlphaFoldDB; C5CHA1; -.
DR SMR; C5CHA1; -.
DR STRING; 521045.Kole_0011; -.
DR EnsemblBacteria; ACR78740; ACR78740; Kole_0011.
DR KEGG; kol:Kole_0011; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_0_0; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002382; 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; 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..921
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_1000216238"
FT MOTIF 57..67
FT /note="'HIGH' region"
FT MOTIF 592..596
FT /note="'KMSKS' region"
FT BINDING 551
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 905
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 908
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 921 AA; 106289 MW; 541E12C0770C7733 CRC64;
MDYKDTLNLP KTSFSMRANL VRKEPEQLKK WEEMDLYKYV QKNREGAPLF VLHDGPPYAN
GNIHVGTALN KILKDFIIKY KTMQGYNAPY IPGWDTHGLP IEHRVASELG EKAKELSKST
IRKKCRKYAE KYVKIQREQF KRLGVRGDWE NPYLTFDPKY EASVLKVLSK LVKSGNVYRT
LKPIYWCTSC ETALAEAEVE YHDHKSYSIY VKFQDKNKPN RFFVIWTTTP WTLPANVAIA
LNPNFDYCEV KVKDEIWILA EGLLEQAMKA MGIESYEIIS TKKGSEFEGE VAQHPFMNRD
SVIVMADYVA LDAGTGCVHT APGHGEEDYG TGLRYRLPVI SPVNDQGIFT KEAGKYAGLF
VFDANPIIVE DLRKSGHLVG EGKIEHSYPH CWRCKNPVIF RATEQWFIDV DKNDLRQKAL
SEIEKTEWHP SWGQNRITAM VQDRPDWCIS RQRSWGIPIP AFRCQDCGES ILDGKVIDHF
AGIVEEKGTD VWFEWSESDL LPEGYTCPKC GSKNLKKQED ILDVWVDSGS SFEAVVKVMD
ELRFPADVYI EGSDQHRGWF QSSLLLSVGT EGVAPFKSVI THGFINDEQG RKMSKSLGNA
VDPQEINNKY GAEILRLWVA SSNYQEDIRI SMNIIQQQIE NYKKIRNTLR YLLGNLSDYS
PQDSVPYEEL LELDKWAIMK LHKLIRDVTR YYDRYEFYKV FQSILKFIIT DMSAFYLDII
KDRLYVEGKT SPERRSAQTV LFEILVALNK MLAPILTFTS EEVYAHLPEA ARNYKTIQVE
NWPEYKEEYI DSSLEERWEK LINLREDVLK ALEIARAEKL IGNSLDAKVT LQIRSKDIDE
IVRQYSREFI ADLFIVSQVE FAESVEGFNG EYAVVKVDRA EGEKCQRCWK YSIETGADPE
LPDMCPRCVA VLRKYGSDYE L
