ID   SYI_BORA1               Reviewed;         953 AA.
AC   Q2L2K5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=BAV1411;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ49020.1; -; Genomic_DNA.
DR   RefSeq; YP_785933.1; -.
DR   GeneID; 6266797; -.
DR   GenomeReviews; AM167904_GR; BAV1411.
DR   KEGG; bav:BAV1411; -.
DR   NMPDR; fig|521.1.peg.474; -.
DR   HOGENOM; Q2L2K5; -.
DR   OMA; Q2L2K5; 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    953       Isoleucyl-tRNA synthetase.
FT                                /FTId=PRO_1000022043.
FT   MOTIF        57     67       "HIGH" region.
FT   MOTIF       623    627       "KMSKS" region.
FT   METAL       916    916       Zinc (By similarity).
FT   METAL       919    919       Zinc (By similarity).
FT   METAL       936    936       Zinc (By similarity).
FT   METAL       939    939       Zinc (By similarity).
FT   BINDING     582    582       Aminoacyl-adenylate (By similarity).
FT   BINDING     626    626       ATP (By similarity).
SQ   SEQUENCE   953 AA;  105398 MW;  65C8B60E800D7C55 CRC64;
     MDYKKTLNLP DTSFPMRGDL AKREPGWVQQ WEENRVYQAI RAASKGRPLF ILHDGPPYAN
     GDIHIGHAVN KILKDIIVKS RSMAGYDAPY VPGWDCHGMP IEIQVEKKFG KNLPVTEVHA
     KARAYALEQL DRQRQDFKRL GVLGDWDNPY LTMNFSNEAD EIRVLARILE KGYVFRGLKP
     VNWCFDCGSA LAEAEVEYAD RVDPAIDVAF PFTDKAALAG AFGLDSVDDG AIVIWTTTPW
     TIPSNQALNV HPEIEYALVR VSPTPVHGPL VLIAKERVEA CLKTWGLEGE IIATAPGQAL
     DGLRFAHPLA RAAEGYDRTS PIYLGDYVTL DTGTGVVHSA PAYGIEDFVS CKNHGLADAD
     ILSPVMGDGK YIATLPLFGG LSIWDANPKI VEALKLAGSL MHVQKLSHSY MHCWRHKSPV
     IYRATSQWFA GMDVTPEGGG QTLRESALAG IEATTFYPAW GRARLQAMIA NRPDWTLSRQ
     RQWGVPMAFF VHKETGALHP RTVELLEEVA KRVEKSGIEA WQSLDPRELL GDEADSYEKN
     RDTLDVWFDS GSTHATVLGG KDHALHGSHG EQLAWPADLY LEGSDQHRGW FHSSLLTGCM
     LYGQPPYKGL LTHGFVVDGQ GRKMSKSVGN VIAPQKVSDS LGAEILRLWV ASTDYSGELS
     ISDEILKRVV EGYRRIRNTL RFLLANVADF DGVNQAVPYG DLLEIDRYAL VMTAQMQAEV
     QAHYQSYDFH PAVSRLQTFC SEDLGAFYLD ILKDRLYTNA PGSHARRSAQ TALLDITQTL
     VKLMAPILSF TAEEAWKVLA DSALKHQADA ARLTIFTEVY HTLPPYADAD ALAGRWGRLR
     AIRADVLRKL EDVRGEGLIG SSLQAEVDIY ADGEDLALLS ALGDDLRFVL IVSRATVHAR
     AGELAIEIAP SAHKKCERCW HWRADVGQDA DHPEICGRCV SNLFGAGESR AKA
//