ID SYI_BACC7 Reviewed; 921 AA.
AC B7HLM9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 35.
DE RecName: Full=Isoleucine--tRNA ligase;
DE EC=6.1.1.5;
DE AltName: Full=Isoleucyl-tRNA synthetase;
DE Short=IleRS;
GN Name=ileS; OrderedLocusNames=BCAH187_A3947;
OS Bacillus cereus (strain AH187).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
RL Submitted (OCT-2008) 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; CP001177; ACJ82513.1; -; Genomic_DNA.
DR RefSeq; YP_002339884.1; NC_011658.1.
DR ProteinModelPortal; B7HLM9; -.
DR STRING; 405534.BCAH187_A3947; -.
DR EnsemblBacteria; ACJ82513; ACJ82513; BCAH187_A3947.
DR GeneID; 7077283; -.
DR KEGG; bcr:BCAH187_A3947; -.
DR PATRIC; 18833323; VBIBacCer120511_4132.
DR eggNOG; COG0060; -.
DR HOGENOM; HOG000246402; -.
DR KO; K01870; -.
DR OMA; KQVLTHG; -.
DR ProtClustDB; PRK05743; -.
DR BioCyc; BCER405534:GHXM-5334-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:0008270; F:zinc ion binding; 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 InterPro; IPR010663; Znf_DNA_glyclase/IsotRNA_synth.
DR PANTHER; PTHR11946:SF9; PTHR11946:SF9; 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 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; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT CHAIN 1 921 Isoleucine--tRNA ligase.
FT /FTId=PRO_1000189127.
FT MOTIF 57 67 "HIGH" region.
FT MOTIF 593 597 "KMSKS" region.
FT METAL 888 888 Zinc (By similarity).
FT METAL 891 891 Zinc (By similarity).
FT METAL 908 908 Zinc (By similarity).
FT METAL 911 911 Zinc (By similarity).
FT BINDING 552 552 Aminoacyl-adenylate (By similarity).
FT BINDING 596 596 ATP (By similarity).
SQ SEQUENCE 921 AA; 104550 MW; 715ABAF58FED9C2E CRC64;
MEYKNTLLMP KTEFPMRGNL PKREPAMQEK WAEMNIYEKV QEHTKGRPLF VLHDGPPYAN
GDIHMGHALN KVLKDFIVRY KSMTGFCAPY VPGWDTHGLP IEQALTNKGV KRKEMTVAEF
RKLCAEYAYE QVERQREQFK RLGVRADWDN PYITLEPAYE AQQIKVFGDM AKKGYIYKGQ
KPVYWSPTSE SALAEAEIEY QDKKSASIYV AFPVKDGKNV LEGDEKYIIW TTTPWTLPAN
LGISVHPELE YAIVKVNGEK YIIASELFET VAKTLEWENA EVVKTVKGSE LEYTVAKHPF
YDRDSLVMLG DHVTTDAGTG CVHTAPGHGE DDFIVGKKYG LEVLCPVDDK GVLTEEAPGF
EGLFYDKANK PITEKLEEVG ALLKLTFITH SYPHDWRTKK PIIFRATAQW FASIEAFRKE
LLEAVAETKW VPAWGETRLH NMVRDRGDWC ISRQRAWGVP IPVFYAENGD PIITDETINH
VADLFREHGS NVWFEREAKD LLPEGFTHSG SPNGEFRKET DIMDVWFDSG SSHQAVLEER
DDLQRPADLY LEGSDQYRGW FNSSLSTAVA VTGKAPYKGV LSHGFVLDGE GRKMSKSIGN
IVVPKKIMDQ LGGDILRLWV SSVDYQSDVR ISDDILKQVA EVYRKIRNTF RFLLGNLDDF
KPSENTVAVA ELREVDRYML VKLNDLITKV KEAYETYDFA AVYHAIHNFC TIDLSSFYLD
FAKDILYIEG ANHEDRRAIQ TVLYDVLVAL TKLVTPILPH TADEVWPYIP GVTEESVQLT
DMPEAVQLDG AEALKTKWDA FMTLRDDVLK ALEVARNEKV IGKSLNASIT LYPTAEMKAM
LESINEDLKQ LFIVSEYKLG GMMEEAPADA PKYEHTAVVV VQATGETCER CWVVSETIGK
DAEHETLCER CATVVKENYV K
//
