ID E3DZS2_BACA1 Unreviewed; 920 AA.
AC E3DZS2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 01-MAY-2013, entry version 22.
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 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:HAMAP.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA: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; tRNAsyn_1a_bind; 1.
DR SUPFAM; SSF50677; ValRS_IleRS_edit; 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
//
