ID   SYI_BAUCH               Reviewed;         938 AA.
AC   Q1LSS9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=BCI_0556;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(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; CP000238; ABF14142.1; -; Genomic_DNA.
DR   RefSeq; YP_588985.1; -.
DR   GeneID; 4056571; -.
DR   GenomeReviews; CP000238_GR; BCI_0556.
DR   KEGG; bci:BCI_0556; -.
DR   HOGENOM; Q1LSS9; -.
DR   OMA; Q1LSS9; 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    938       Isoleucyl-tRNA synthetase.
FT                                /FTId=PRO_1000022042.
FT   MOTIF        58     68       "HIGH" region.
FT   MOTIF       602    606       "KMSKS" region.
FT   METAL       901    901       Zinc (By similarity).
FT   METAL       904    904       Zinc (By similarity).
FT   METAL       921    921       Zinc (By similarity).
FT   METAL       924    924       Zinc (By similarity).
FT   BINDING     561    561       Aminoacyl-adenylate (By similarity).
FT   BINDING     605    605       ATP (By similarity).
SQ   SEQUENCE   938 AA;  107240 MW;  697B57DCEEB6DAAA CRC64;
     MIDYKNTLNL PKTQFAMRGN LAIREPIMLK RWHQQDLYQL ICQATQGKKT FFLHDGPPYA
     NGSIHIGHSV NKILKDIIIK SKRLMGYCSP YIPGWDCHGL PIELKVEQLI GKPGKKVSAS
     EFIIACRNYA SEQVTWQKKD FIRLGVLGDW DNIYRTMDFH TEANIIRTLS KIIENGHVYQ
     GNKPVHWCID CRSALAEAEV EYYDYTSPSI YVIFAATNTH DVAARFGIPN VLSSISFLVW
     TTTPWTIPAN RAISIHPNLN YQLVKVNQQG FILAADLVTS VLTYLGIQNW TVVKNIKGYV
     LELLRFSHPF MKFDVPVVLS NHVTINVGTG VVHTSPSHGP DDYLIGREYN LEIVNIVGPD
     GCYLPGTFSL LDGTSVYQSN QTVISLLKDR GALLHTGTIQ HSYPHCWRHK TPLIFRATPQ
     WFISMDKKKL RQQSLKEIKK IQWIPSNSQA SITNMVNNRQ DWCISRQRIW GVPMSLFVHN
     HTKKLHPQTS EIMEYVAKQV EKKGIQAWWD LDPIKILGDD IVNYSKINDI LDVWFDSGST
     HSSVINAQTE FANHEIDMYL EGADQHRGWF MSSLISSTAI KGKAPYKTVI THGFAVDSNG
     RKMSKSIGNV VSPQQVVDKL GADILRLWVA STNYTDDMTI SDEILKRSVD TYRRIRNTAR
     FLLANLNGFE PKQHSVSIDK MIILDQWAID RAQVAQDEII AAYNSYEFHS VVQRIMQFCS
     VEMGSFYLDI IKDRQYTTQY NSIARRSCQT ALFHIIEAMV RWIAPIISFT ADEIWGFIPG
     KRSPSVFIEE WYKNLSRLDA EQHMNDTYWN TLLQVRSDVN YLIEQARIKK NIGSSLETQV
     TLYSEPILAM QLRQLGNELH FVLLTSAVQI ADYQEADNNA LQSTRIKGLK ITLNHATGRK
     CQRCWHYEQD IGNNTQYPEI CGRCVINIAG NGEERKFV
//