ID   SYI_BUCCC               Reviewed;         941 AA.
AC   Q057X9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=BCc_093;
OS   Buchnera aphidicola subsp. Cinara cedri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=372461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17038625; DOI=10.1126/science.1130441;
RA   Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M.,
RA   Michelena J.M., Silva F.J., Moya A., Latorre A.;
RT   "A small microbial genome: the end of a long symbiotic relationship?";
RL   Science 314:312-313(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; CP000263; ABJ90570.1; -; Genomic_DNA.
DR   RefSeq; YP_802663.1; -.
DR   GeneID; 4440638; -.
DR   GenomeReviews; CP000263_GR; BCc_093.
DR   KEGG; bcc:BCc_093; -.
DR   OMA; Q057X9; 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    941       Isoleucyl-tRNA synthetase.
FT                                /FTId=PRO_1000022044.
FT   MOTIF        58     68       "HIGH" region.
FT   MOTIF       605    609       "KMSKS" region.
FT   METAL       904    904       Zinc (By similarity).
FT   METAL       907    907       Zinc (By similarity).
FT   METAL       924    924       Zinc (By similarity).
FT   METAL       927    927       Zinc (By similarity).
FT   BINDING     564    564       Aminoacyl-adenylate (By similarity).
FT   BINDING     608    608       ATP (By similarity).
SQ   SEQUENCE   941 AA;  112919 MW;  D00F6241B1F556BC CRC64;
     MINIKKSLNL PKTKFPMKAN LAYKENEILE TWKKINLYNK LHKNKKKNKQ FFLQDGPPYA
     NGNIHIGHAV NKILKDIILK FKRMSGFFSP YIPCWDCHGL PIEHIIEKKL SKKKINKKEF
     RKICFKYVLK QVEKQKNDFI RLGIIANWDN INLSTDYINQ SNTIKVLTKI VEKGLIYRDL
     KPVYWCFDCQ SALAEAEIEY KFKKSISIYI EYKLIENSIL KNNFFKNYNK KIFNNISILI
     FTTTPWTIPT CQAIAINPKL YYQIIKINKK YYICIEELTK KIFKKNNIKK WKIILSFKGK
     EIEHIKCFHP FLNTQIPIIL SKHVSNQLGT GAVHMSPDHG YEDFIACKKY KIIPKQIVDS
     HGFYKIKKYS QLNNIHIFNK ENKIIYILKK NKKLFFFQTI NHNYPHCWRH KKPIIFRATP
     QWFINLSKKN FKEDTFNKIK KILWIPSWGK NKMKKMLKIR PDWCISRQRI WGIPLPFFIH
     KNTGELHPNT VMIMKKIVKK IRNHGYKIWW ESNVNTWIKK DSETYRKVND VLDVWFESGA
     NHQLKIYKHN IKNKKNYVAD LYLEGSDQHR GWFMSSLIIS MITKTIPPYL SVITHGFVLD
     KNGQKMSKSL NNNISPKKII QKKGADILRL WVAYTNYTND ISISNEILEQ ISDNYRRIRN
     TIRFLFSNIF DFKANIHIIK YEKMLFLDQW IIEKTYNYQR KIIKKYSQYQ FHKVIKKIIN
     FCSIELGSCY LELIKDRQYT MHKNSIERRS SQTAIFYILQ FLVRWIAPIL SFTAEEIWSQ
     LQEKKEKSIF MTQWYKNKQL IKKKSTYNLF FWKKIFAIRK EINLFIETEK KNKFIKNSLE
     IILLLYINKK LFNFLLLFNN ELKFIFLVSE TQLHKYSSAP SLAIKSKKIK KFKILIKKSK
     KIKCPRCWNY TKKNNFLKNK NSICNKCIKN INQTNKKHIF L
//