(data stored in ACNUC7421 zone)

SWISSPROT: SYI_EDWI9

ID   SYI_EDWI9               Reviewed;         948 AA.
AC   C5B7M4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 57.
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};
GN   OrderedLocusNames=NT01EI_0679;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As
CC       IleRS can inadvertently accommodate and process structurally
CC       similar amino acids such as valine, to avoid such errors it has
CC       two additional distinct tRNA(Ile)-dependent editing activities.
CC       One activity is designated as 'pretransfer' editing and involves
CC       the hydrolysis of activated Val-AMP. The other activity is
CC       designated 'posttransfer' editing and involves deacylation of
CC       mischarged Val-tRNA(Ile). {ECO:0000255|HAMAP-Rule:MF_02002}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP +
CC       diphosphate + L-isoleucyl-tRNA(Ile). {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-
CC       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
CC       aminoacylation and one for editing. The misactivated valine is
CC       translocated from the active site to the editing site, which
CC       sterically excludes the correctly activated isoleucine. The single
CC       editing site contains two valyl binding pockets, one specific for
CC       each substrate (Val-AMP or Val-tRNA(Ile)). {ECO:0000255|HAMAP-
CC       Rule:MF_02002}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}.
DR   EMBL; CP001600; ACR67901.1; -; Genomic_DNA.
DR   RefSeq; WP_015870094.1; NC_012779.2.
DR   ProteinModelPortal; C5B7M4; -.
DR   STRING; 634503.NT01EI_0679; -.
DR   EnsemblBacteria; ACR67901; ACR67901; NT01EI_0679.
DR   GeneID; 7962013; -.
DR   KEGG; eic:NT01EI_0679; -.
DR   PATRIC; fig|634503.3.peg.611; -.
DR   eggNOG; ENOG4105C07; Bacteria.
DR   eggNOG; COG0060; LUCA.
DR   HOGENOM; HOG000246402; -.
DR   KO; K01870; -.
DR   OMA; ATEQWFI; -.
DR   OrthoDB; POG091H028I; -.
DR   Proteomes; UP000001485; 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-KW.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   Gene3D; 1.10.730.10; -; 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;
DR   PRODOM; C5B7M4.
DR   SWISS-2DPAGE; C5B7M4.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; Zinc.
FT   CHAIN         1    948       Isoleucine--tRNA ligase.
FT                                /FTId=PRO_1000216235.
FT   MOTIF        58     68       "HIGH" region.
FT   MOTIF       613    617       "KMSKS" region.
FT   METAL       911    911       Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}.
FT   METAL       914    914       Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}.
FT   METAL       931    931       Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}.
FT   METAL       934    934       Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}.
FT   BINDING     572    572       Aminoacyl-adenylate. {ECO:0000255|HAMAP-
FT                                Rule:MF_02002}.
FT   BINDING     616    616       ATP. {ECO:0000255|HAMAP-Rule:MF_02002}.
SQ   SEQUENCE   948 AA;  105791 MW;  2399B079470C2A0C CRC64;
     MSDYKNTLNL PETGFPMRGD LAKREPGMLQ HWYEQDLYGI IRNAKQGKKS FILHDGPPYA
     NGSIHIGHSV NKILKDIIIK SKGLSGYDSP YIPGWDCHGL PIELKVEQLI GKPGEKYSAA
     EFREQCRAYA AEQVAGQKAD FIRLGVLGDW EHPYLTMDYG TEANIIRALA RIVDNGHLMK
     GAKPVHWCPD CGSSLAEAEV EYYDKVSPSI DVRFAAVDKA QVLAKFGVSE AKGDVNVVIW
     TTTPWTLPAN RAVALHPELE YQLVQVEGEC LILAADLVES VMKRAGIDYW QVLGSCKGEA
     LELLHFCHPF MNFDVPIIMG DHVTLDAGTG AVHTAPGHGP DDYVVGQKYG LEIANPVGSN
     GCYLPGTHPV LDGLFVFKAN DIVIDLLKDS GALLHVEKLT HSYPCCWRHK SPIIFRATPQ
     WFISMDRQGL RSQSLAEIDR IERQGLDEQN LSGWIPAWGK ARIESMVANR PDWCISRQRT
     WGVPMAMLVH KETQELHPRT TELMEMVAKR VEQAGIQAWW DLDIRDLLGD EADQYEKVPD
     TLDVWFDSGS TSYSVVDARP EFNGHSPDMY LEGSDQHRGW FMSSLMISVA MKGKAPYRQV
     LTHGFTVDGQ GRKMSKSVGN VVSPQQVMNK LGGDILRLWV ASTDYTSEMA VSDEILKRSA
     DAYRRIRNTA RFLLANLNGF DPCKDMVKPE DMVVLDRWAV GCAKQAQDEI IAAYENYDFH
     EVVQRLMQFC SVEMGSFYLD IIKDRQYTAK ADSVARRSCQ TALYHIAEAL VRWMAPILSF
     TADEVWGYLP GDRAQFVFTE EWYQGLFGLD AAEQMNDAFW AELLKVRGEV NRVIEQARND
     KKVGGSLEAA ITLYADEALA TQLDSLQDEL RFVLITSAAR VQPLVQATAD AVASELAGLK
     VGLGKADGSK CPRCWHYSTA IGQDAAHPQL CPRCVTNVAG QGEERKFA
//

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