ID   SYI_BLOPB               Reviewed;         942 AA.
AC   Q493S3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Isoleucyl-tRNA synthetase;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucine--tRNA ligase;
DE            Short=IleRS;
GN   Name=ileS; OrderedLocusNames=BPEN_122;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP +
CC       diphosphate + L-isoleucyl-tRNA(Ile).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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)) (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. IleS type 1 subfamily.
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DR   EMBL; CP000016; AAZ40762.1; -; Genomic_DNA.
DR   RefSeq; YP_277635.1; -.
DR   GeneID; 3563125; -.
DR   GenomeReviews; CP000016_GR; BPEN_122.
DR   KEGG; bpn:BPEN_122; -.
DR   HOGENOM; Q493S3; -.
DR   OMA; Q493S3; FPMRGNL.
DR   BioCyc; CBLO291272:BPEN_122-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_02002; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR010663; DNA_glyclase/IsotRNA_synth_Znf.
DR   InterPro; IPR002301; Ile-tRNA-synt_Ia.
DR   InterPro; IPR015905; Ile-tRNA-synt_Ia_N.
DR   InterPro; IPR018353; Isoleucyl-tRNA_synthetase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11946:SF9; Ile-tRNA-synt_Ia; 1.
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   TIGRFAMs; TIGR00392; ileS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN         1    942       Isoleucyl-tRNA synthetase.
FT                                /FTId=PRO_0000098356.
FT   MOTIF        58     68       "HIGH" region.
FT   MOTIF       605    609       "KMSKS" region.
FT   METAL       905    905       Zinc (By similarity).
FT   METAL       908    908       Zinc (By similarity).
FT   METAL       925    925       Zinc (By similarity).
FT   METAL       928    928       Zinc (By similarity).
FT   BINDING     564    564       Aminoacyl-adenylate (By similarity).
FT   BINDING     608    608       ATP (By similarity).
SQ   SEQUENCE   942 AA;  108694 MW;  D9724149300EDD20 CRC64;
     MINYKNTLNL PYTLFPMRAN LPVCEPTILE RWYKDNLYEA IRHKKSKKKL FILHDGPPYV
     NGSIHLGHAV NKVLKDIILK YKTLTGYNAP YIPGWDCHGL PIELQVERLI GQLGVNVDPN
     EFRSICRNYV LDQIEIQKKD FVRLGVLGDW SRPYLTMDFK TEANIIRTLS KVISNGYFYK
     GTKPVHWCFQ CCSVLAESEV EYNNHCSPAI DVAFFAVDNI RISKIFNIDL CQRVIELVIW
     TTTPWTLPSN QAISVHPDYS YQLIAINNSK YIIIAANLVN TVMQRIQCFS WRILGETSGN
     SLESLKFRHP FMSFDVPVVL SGHVALDSGT GVVHIAPNHG VDDYIIARKY NFKIVNIINE
     TGHYVSNVHP MLDGVQVFQS NEIIIKLLNQ SGSLLHVNHN YKHNYPYCWR HAVPVIFKAT
     AQWFLSMDKY NLRNKLLQTI HQVDWIPNKG EYSIETMIVN RPDWCLSRQR VWGVPIPLFI
     HKKTSILHPR TIALMEVIAQ HVEQNGIQAW WDLKTEDIID NEEADQYEKV LDTLDVWFDS
     GSTHYSVIPE RLEYRKQSPD LYLEGSDQYR GWFMSSLIIS TVITGQAPYR EVLTHGFTVD
     AQGRKMSKSL GNVISPQEII KDFGADILRL WIASSDYSKE MAISNAILKH TIDVYRRIRN
     TARFCLANIS DFDPEKDSVH PENMIELDCW AIDRALSVQL EVISDYNKYN FHNVIQRIMQ
     FCSVEMGSFY LDVIKDRQYT TKKNSKERRS CQTALYHIIE SMVRWIAPVL SFTADEIWRH
     IPGNRSKYVF TEEWYNGLFS ISSKQIMNSH DWNTFLNVRS EVNKIVEQTR LNGIIGGSLD
     ASVVLYATPE LANTLRILGN ELSFGLITSS AIVSDYCNGF NVTQYTQEGI PGLKIFLEKA
     KGKKCLRCWH YRLDIGQYKN YSNICARCVN NIVGPGEKRR FF
//