ID   SYI_BURCM               Reviewed;         945 AA.
AC   Q0BCK8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=Bamb_2559;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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) (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; CP000440; ABI88115.1; -; Genomic_DNA.
DR   RefSeq; YP_774449.1; -.
DR   GeneID; 4308894; -.
DR   GenomeReviews; CP000440_GR; Bamb_2559.
DR   KEGG; bam:Bamb_2559; -.
DR   NMPDR; fig|339670.3.peg.3368; -.
DR   OMA; Q0BCK8; FPMRGNL.
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    945       Isoleucyl-tRNA synthetase.
FT                                /FTId=PRO_1000022047.
FT   MOTIF        66     76       "HIGH" region.
FT   MOTIF       622    626       "KMSKS" region.
FT   METAL       908    908       Zinc (By similarity).
FT   METAL       911    911       Zinc (By similarity).
FT   METAL       928    928       Zinc (By similarity).
FT   METAL       931    931       Zinc (By similarity).
FT   BINDING     581    581       Aminoacyl-adenylate (By similarity).
FT   BINDING     625    625       ATP (By similarity).
SQ   SEQUENCE   945 AA;  105855 MW;  A483E1C0822BCD44 CRC64;
     MSNKKADSKP QAKYPVNLLD TPFPMRGDLP KREPQWVKEW EERGIYEKIR AASKGRPKFI
     LHDGPPYANG DIHLGHAVNK ILKDIVVKSR NMAGFDAPYV PGWDCHGMPI EIQIEKQFGK
     SLPAAEVMSK ARAYATEQIE KQKVGFKRLG VLGDWANPYK TMNFVNEAEE IRALGKIIEK
     GYVYRGLKPV NWCFDCGSAL AEAEVEYKDR TDPTIDVMFA FAEPEKTAQA FGLPALPRAE
     GGIVIWTTTP WTIPANQALN LHPEIVYALV DTERGLLIIA EERVAACMAD FKLTGRVVAT
     APGVKLANLR FHHPLASAHP GYKRTAPVYL GDYVTTDTGT GVVHSSPAYG IEDFMSCKAH
     GMTDSDFINP VMGDGRYIES LPLFGGLSIW DANPKIVDAL NAAGSLLRSE KYTHSYMHCW
     RHKTPIIYRA TSQWFAGMDV TPRDDGKTLR EAALEGVEAT AFYPSWGKQR LFSMIANRPD
     WTLSRQRQWG VPMAFFVHKE TGELHPRTLE LLEEVAKRVE QSGIEAWQSL DPRELIGDDA
     NMYEKNRDTL DVWFDSGTTH WHVLRGSHKD QLQFPADLYL EGSDQHRGWF HSSLLTASMI
     DGRAPYKGLL THGFTVDGEG RKMSKSLGNG VDPHEVANRL GAEIIRLWIA STDYSGELAI
     SEEILKRVTE GYRRIRNTLR FLLANLSDFD FAQHAVPVDE WLEIDRYAVA FSAQLQTELL
     GHYEKYEFHP VVAKLQTYCS EDLGGFYLDV LKDRLYTSAA DSRARRSAQT ALYHLTHGLL
     RVLAPFLSFT AEEAWKVFQP ASDTVFTETY YAYPEVAGSA ALIEKWALLR DVRGNVTKAL
     EEARTANRIG SSLQAEVAVH ASGARYDALT SLGDDLKFVL ITSAATVVKV DDEAQESVDV
     AASKYQKCER CWHYREDVGA HADHPTLCGR CFSNLFENGE IRSAA
//