ID D5X7Y7_THEPJ Unreviewed; 934 AA.
AC D5X7Y7;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 29-MAY-2013, 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=TherJR_1858;
OS Thermincola potens (strain JR).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC Thermincola.
OX NCBI_TaxID=635013;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JR;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.;
RT "Complete sequence of Thermincola sp. JR.";
RL Submitted (MAY-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 -!- 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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP002028; ADG82707.1; -; Genomic_DNA.
DR RefSeq; YP_003640608.1; NC_014152.1.
DR ProteinModelPortal; D5X7Y7; -.
DR EnsemblBacteria; ADG82707; ADG82707; TherJR_1858.
DR GeneID; 9149546; -.
DR KEGG; tjr:TherJR_1858; -.
DR PATRIC; 38275383; VBITheSp141296_1989.
DR HOGENOM; HOG000246402; -.
DR KO; K01870; -.
DR BioCyc; TPOT635013:GHIM-1899-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 MOTIF 57 67 "HIGH" region (By similarity).
FT MOTIF 604 608 "KMSKS" region (By similarity).
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 563 563 Aminoacyl-adenylate (By similarity).
FT BINDING 607 607 ATP (By similarity).
SQ SEQUENCE 934 AA; 106770 MW; A09C55C0A91699DD CRC64;
MDYSKTLNLP QTEFPMRANL SEREPEILKF WEDNSIYKKV QEKNAGKEKF ILHDGPPYAN
GDIHLGHTLN KVLKDIIVKF KSMDGFDAPF VPGWDTHGLP IEQQAIKALG INRHEVGPVE
FRKKCKEYAL KYVDIQREQF KRLGCRGDWD NPYLTLQPHF EAKQIEVFGE MAKKGYIYKG
LKPVYWCASC ETALAEAEIE YAEKKSASIY VKFAVKDGKG VLPEDNTFVV IWTTTPWTIP
ANVAIAVHPD FEYSLVEVKD SERKGERYVI AKEMLAGVMD VFDIKFYDEL KTIRGQELEY
VVCKHPLIER DSLVILGEHV TLEAGTGAVH TAPGHGLEDF EIGKVYNLPV INPIDNKGRF
TEEGGIFCGQ DTNEGNKNVV IELDKVGALL KLEWIRHQYP HCWRCKNPIL FRATEQWFAS
IDGFRKEALE AIKEVQWIPT WGEDRIHNMI ADRGDWCISR QRTWGVPIPI FYCEACGKDL
INDATIKHVA GLFRKYGSDV WFARDAKDLL PEGTKCPSCG RTEFRKETDI MDVWFDSGSS
HKAVLEQPEI WPDLRWPADL YLEGSDQHRG WFNSSLCTSV ATTGKAPYKT VLTHGFLVDE
QGRKMSKSLG NGIDPLEVIN KMGADILRLW VSSADYKADV ALSSNILKQM SEAYRKIRNT
ARYILGNLYD FDPAKDTVPY EQMEELDKWA LLKLHKLSKR VLNAYRNYEF HILYHAIHNF
CAVDMSAFYL DIIKDRLYTS LPSSVERRAA QTVMYEIINT LVRLIAPVLS YTAEEIWRYI
PYKEENLISV QLADMPKVNE AYLDQALEDK WEKVIKIREE VAKELEKARR DKVIGHSLNA
QVHIYPDEKL RAFLAPLQEQ LATIFIVSSV QIHEPEEVLP EAASVSEEVP GLAVTVNQAP
GEKCERCWVY SPEVGKNADH PSICPRCAEV VAQL
//
