ID   SYI_BORAP               Reviewed;        1042 AA.
AC   Q0SM18;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=BAPKO_0886;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(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: Zinc (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 2 subfamily.
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DR   EMBL; CP000395; ABH02110.1; -; Genomic_DNA.
DR   RefSeq; YP_710286.1; -.
DR   GeneID; 4227163; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0886.
DR   KEGG; baf:BAPKO_0886; -.
DR   NMPDR; fig|390236.5.peg.888; -.
DR   HOGENOM; Q0SM18; -.
DR   OMA; Q0SM18; SNWYVRR.
DR   BioCyc; BAFZ390236:BAPKO_0886-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:HAMAP.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_02003; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
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   PRINTS; PR00984; TRNASYNTHILE.
DR   TIGRFAMs; TIGR00392; ileS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG.
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   1042       Isoleucyl-tRNA synthetase.
FT                                /FTId=PRO_1000022148.
FT   MOTIF        48     58       "HIGH" region.
FT   MOTIF       594    598       "KMSKS" region.
FT   BINDING     597    597       ATP (By similarity).
SQ   SEQUENCE   1042 AA;  122522 MW;  51B78BF0D7E1C44F CRC64;
     MFKKVENKAN FPKIEEKILK FWNDNKIFEK SMKQREGCEE FTFYDGPPFA TGLPHFGHFV
     PNTIKDIIPR YQTMRGKYVK RNFGWDTHGL PVEYEVEKKL GISGKYEIEN YGIENFNKEC
     KKIVLRYTEE WKNIILRLGR WVDFEKGYKT MDINFMESVW WVFKSLYNKG LIYESYYVLP
     YSPKLATPLS NFEVNLGEYK EVNDPSLTIK FKIKDKNEYL LAWTTTPWTL PSNLGIAVGQ
     EIEYSKIFDK KKEEILILGS KKLDSYYDDE NSYTIIEKFK GSKLEGIEYE PIFNYFLEQK
     DKGAFKVHMA DYVTTDDGTG IVHIAPFGEE DYRILKKHTN VDIIDPLDAE CKFTNRVKDF
     QGLFVKDADK KIIENLKLRN FLFKRENYLH RYPFCYRTNY PIIYRPISSW FVNVEKIKTK
     LLEVNEKINW MPAHLKKGRF GKWLENAKDW AISRNRFWGN PIPIWICSKT GKKICVGSKK
     ELESLSGQKI EDLHKDKVDK ITWPSKDGGT FIRTSEVLDC WFESGAMPYA SNHYPFTNES
     NFKNIFPADF IAEGLDQTRG WFYTLTILGV SLFESTAFKN VIVNGLVLSS DGRKMSKSFK
     NYTDPMEVIN TFGADALRLY LIMSPVVKAD DLKYSDNGVR DVLKNIIIPI WNAYSFFTTY
     AIIDKFQPPK NLNLVKNNNL DKWIISELES LKKILNNEID KYNLTKSIES LLEFIDKLNN
     WYIRRSRRRF WKSENDKDKN DAYETLYYAI KTLMILLAPF IPFITEEIYQ NLKTDEDKQS
     IHLNDYPKAN ENLINKTIEE KINLARKITS MARSLRSLHN IKIRMPISMI YIVTKNQNEQ
     NMLIEMQEII LDEINAKEMK IKSNEEDLIT YKAKANFKEL GKKLGKDMKT VSIEISKLKN
     EDIIKIINGI SYEIKVGNTK YYLSLNDIIL EREEKDNLKV INEESITIGI DSLITKELYL
     EGLTREFVRQ IQNLRKEKNF DVSDRINLYI ENNETLQEIL NKFEKYIKTE TLALNIIFNK
     SKLEKKINLD DNIFTIIGIE KC
//