SYI_COREF
ID SYI_COREF Reviewed; 1054 AA.
AC Q8FNV0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 116.
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=CE2043;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=BAC18853.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000035; BAC18853.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011075728.1; NZ_GG700683.1.
DR AlphaFoldDB; Q8FNV0; -.
DR SMR; Q8FNV0; -.
DR STRING; 196164.23493885; -.
DR EnsemblBacteria; BAC18853; BAC18853; BAC18853.
DR KEGG; cef:CE2043; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_11; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001409; 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 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; Reference proteome; Zinc.
FT CHAIN 1..1054
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098537"
FT MOTIF 58..68
FT /note="'HIGH' region"
FT MOTIF 627..631
FT /note="'KMSKS' region"
FT BINDING 630
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1054 AA; 118226 MW; 17924A0E38AF555F CRC64;
MTEAVGGVYP LVDMTGGSSR FPEMEENVLD FWKRDDTFQA SIDQRNDAED YVFYDGPPFA
NGLPHYGHLL TGYVKDIVPR YQTMRGYRVP RVFGWDTHGL PAELEAEKQL GIKDKGEIES
MGLAQFNDYC AKSVLQYTKE WEEYVTRQAR WVDFENGYKT MDLTYMESVI WAFKELYDKG
LIYQGFRVLP YSWAEHTPLS NQETRLDDSY KMRQDPTLTV TMPITGKIEG TGANEALIGA
NAIAWTTTPW TLPSNLALAV NPSVTYALVE VAGDGEEGFV GQQLLLARDL VGAYAKELGT
DARIISEHPG TELIGLTYEP VFDFFRDHPN AFQILGADYV TTEDGTGIVH QAPAFGEDDM
NVCNAADIAP VIPVDMDGKF TSLTPEYEGQ LVFDANKDII RDLKAKGRVF RHQTIEHSYP
HSWRSGEPLI YMALPSWFVN VTKIRDRMVE TNQDIEWMPA HIRDGQFGKW LEGARDWNIS
RSRYWGSPIP VWVSDDENYP RVDVYGSLDE LEADFGVRPT SLHRPYIDEL TRPNPDDPTG
KSTMRRVPDV LDVWFDSGSM PFAQVHYPFE NKDWFDTHAP ADFIVEYIGQ TRGWFYLLHV
LSVGLFDRPA FKKVVAHGIV LGDDGLKMSK SKGNYPNVTE VFDRDGSDAM RWFLMSSPIL
RGGNLIVTEK GIREGVRQAQ LPMWNAYSFL QLYASKKATW SVDSTDVLDR YILAKLHDLV
ADVTAALDAT DIARACDQVR WFCDALTNWY VRRSRDRFWA GDEAHPEAFN TLYTVLETLT
RVAAPLLPMT TEVIWRGLTG ERSVHLTDFP SADSFPADAD LVRTMDEIRG VCSAASSIRK
AHKLRNRLPL PNLTVALPDS GRLADFLSII RDEVNVKNVD LTSDVDAVGT FEVVVNAKVA
GPRLGKDVQR VIKAVKAGNY ERVGETVVAD GIELQDGEYT ERLVAANPDS TAQIDDVDGL
VVLDMEVTPE LEAEGWAADV IRGLQDARKS SGFEVSDRIQ VTLSVPGDKQ EWATRHADHI
AGEVLATSFE VTQDDLGEDA HEVLKGVTAS VARV
