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Database: UniProt/TrEMBL
Entry: E3DZS2_BACA1
LinkDB: E3DZS2_BACA1
Original site: E3DZS2_BACA1 
ID   E3DZS2_BACA1            Unreviewed;       920 AA.
AC   E3DZS2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   19-FEB-2014, entry version 24.
DE   RecName: Full=Isoleucine--tRNA ligase;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucyl-tRNA synthetase;
GN   Name=ileS; OrderedLocusNames=BATR1942_05510;
OS   Bacillus atrophaeus (strain 1942).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=720555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1942;
RA   Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C.,
RA   Bruce D., Karavis M., McGregor P., Hong C., Park K.H., Akmal A.,
RA   Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA   Lindquist J., Liem A., Fochler E., Tapia R., Bishop-Lilly K.,
RA   Detter C., Han C., Sozhamannan S., Rosenzweig C.N., Skowronski E.;
RT   "Genomic signatures of strain selection and enhancement in Bacillus
RT   atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL   Submitted (SEP-2010) 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   -!- 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; CP002207; ADP32056.1; -; Genomic_DNA.
DR   RefSeq; YP_003972987.1; NC_014639.1.
DR   EnsemblBacteria; ADP32056; ADP32056; BATR1942_05510.
DR   GeneID; 9891091; -.
DR   KEGG; bae:BATR1942_05510; -.
DR   PATRIC; 42569028; VBIBacAtr152324_1127.
DR   HOGENOM; HOG000246402; -.
DR   KO; K01870; -.
DR   OMA; VLGDWDN; -.
DR   BioCyc; BATR720555:GHTA-1123-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006450; P:regulation of translational fidelity; IEA:GOC.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023585; Ile-tRNA-ligase_type1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   PANTHER; PTHR11946:SF9; PTHR11946:SF9; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
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; Nucleotide-binding; Protein biosynthesis.
FT   MOTIF        57     67       "HIGH" region (By similarity).
FT   MOTIF       594    598       "KMSKS" region (By similarity).
FT   BINDING     553    553       Aminoacyl-adenylate (By similarity).
FT   BINDING     597    597       ATP (By similarity).
SQ   SEQUENCE   920 AA;  104512 MW;  D0DD4A15FE94F1EF CRC64;
     MDYKDTLLMP KTDFPMRGNL PNREPEMQKQ WEEQDIYRLV QERTKDRPKF VLHDGPPYAN
     GDIHMGHALN KILKDFIVRY KSMSGYNAPY VPGWDTHGLP IETALTKNKK VKRKEMSVAE
     FRKLCEEYAW QQIEGQREQF KRLGVRGDWE NPYVTLKPEY EAQQIRVFGE MAKRGYIYKG
     LKPVNWSPSS ESALAEAEIE YQDKRSASIY VAFAVKDGKG VLENGERIII WTTTPWTIPA
     NLGISVHPDL EYSVISVGGD RFVAASALVE NVASACGFEQ YEVLKTLKGK ELENIVAEHP
     LYGRDSLVML GDHVTTDAGT GCVHTAPGHG EDDFIVGQKY GLDVLCPVDE KGVMTSEAPG
     FEGMFYDDAN KAITQQLEEK GALMNLEFIT HSYPHDWRTK KPTIFRATAQ WFASIKDFRT
     DLLDAIKETK WVPEWGEQRL HNMVRDRGDW CISRQRAWGV PIPVFYAENG EPIITDETIE
     HVSALFREHG SNIWFEKEAK DLLPEGFTHP GSPNGKFTKE QDIMDVWFDS GSSHQAVLEE
     RDDLVRPADL YLEGSDQYRG WFNSSLSTAV AVTGQAPYKG VLSHGFALDG EGRKMSKSIG
     NVVVPAKVMK QLGADILRLW VSSVDYQADV RVSDAILKQV AEVYRKIRNT FRFLHGNLFD
     FDPKANAVAV EDLREVDQYI LVKLNKLIDK VKKAYDEYEF AVVYHSIHNF CTVELSSFYL
     DFAKDVVYIE HADHPDRRSM QTVFYETLLA LAKLTAPILP HTTDELWAHL TFVEEQSVQL
     TDMPEAVAIP NGEAVEEKFD HFMELRNDVL KALETARNEK IIGKSMEASL TLYPNKASQE
     LLSAIKEDVK QLFIVSELTI SEQEAPADAQ SFDSGKIVVE KAEGEMCERS RVISKDVGAN
     PKYPTLSLRN AEIVEKYYQK
//
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