ID   SYI_ALHEH               Reviewed;         941 AA.
AC   Q0AAD1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-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=Mlg_0852;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
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., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
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; CP000453; ABI56206.1; -; Genomic_DNA.
DR   RefSeq; YP_741696.1; -.
DR   GeneID; 4270789; -.
DR   GenomeReviews; CP000453_GR; Mlg_0852.
DR   KEGG; aeh:Mlg_0852; -.
DR   NMPDR; fig|187272.6.peg.822; -.
DR   HOGENOM; Q0AAD1; -.
DR   OMA; Q0AAD1; 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_1000022040.
FT   MOTIF        58     68       "HIGH" region.
FT   MOTIF       603    607       "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     562    562       Aminoacyl-adenylate (By similarity).
FT   BINDING     606    606       ATP (By similarity).
SQ   SEQUENCE   941 AA;  105903 MW;  2B8F9AE6731EAC86 CRC64;
     MSDYKHTLNL PKTGFPMRGN LAKREPERLA GWYQTDLYGR LRRERAGKPR FVLHDGPPYA
     NGDIHIGHAV NKILKDIIIK ARSMDGYDVP YVPGWDCHGL PIELMVEKKR GKAGAKVSPR
     AFRDACREFA ASQVDGQRED FKRLGVLGDW DNPYLTMDYR TEADILRALG RIIQRGHVTR
     GFKPVHWCAD CGSALAEAEV EYEEKTSPAI DVRFAVLEPE ELDRRAGLGG EAAAAGRVAI
     PIWTTTPWTL PANQAVALHP ELEYVVVAFD DELLVLAAEL VESAMARYEV DDYRVVGRCD
     GAVLEGLRLA HPFLEREVPV ILGGHVTTDG GTGAVHTAPG HGQDDYVVGQ QYDLPTDNPV
     DGNGVFLPDT PFFAGQHVFK ANPKVVDLLA ERGALLHHEP YRHSYPHCWR HKTPILFRAT
     PQWFISLDKA GMREHAMAAI KGVSWHPEWG QARIESMVNG RPDWCISRQR NWGVPIALFV
     DKRSGEPHPE SERLIEAVAR RVEEAGVDAW FELDPAELLG ADAERYEKVT DILDVWFDSG
     VTHATVLERR DELQVPADLY LEGSDQHRGW FQSSLLTSVG VRETAPYKGV LTHGFTVDEK
     GHKMSKSRGN VVAPQKVMDT LGADILRLWV ASSDYSAEMA VSDGILKRTA DAYRRMRNTA
     RFLLANLNGF EPAEHAVAPP DMLPLDRWAV DRAYLLQQQV REAYERYEFH RIYQMVHNFC
     VVDLGGFYLD VIKDRQYTTK PDSLARRSCQ TALWHVAEGL VRWLAPIISF TAEEIWEHLP
     GERSDSVLLE TWYEGLFPLD DSDPFGRAFW DDVLAVRAGV NRELEQLRND KVIGASLQAE
     VQLFCPPELK AKLDRLGDEL RFVLITSEAR VEDLERAPVE SVEVPGENGQ GFRLFAAASQ
     HPKCTRCWHH RPDVGHHADH PELCGRCVSN VDGEGETRHY A
//