ID A0A328WGZ0_PAELA Unreviewed; 1029 AA. AC A0A328WGZ0; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 19-JAN-2022, entry version 12. DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02003}; DE EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02003}; DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02003}; DE Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02003}; GN Name=ileS {ECO:0000256|HAMAP-Rule:MF_02003}; GN ORFNames=DP091_04350 {ECO:0000313|EMBL:RAR45523.1}; OS Paenibacillus lautus (Bacillus lautus). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus. OX NCBI_TaxID=1401 {ECO:0000313|EMBL:RAR45523.1, ECO:0000313|Proteomes:UP000249305}; RN [1] {ECO:0000313|EMBL:RAR45523.1, ECO:0000313|Proteomes:UP000249305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MDMC362 {ECO:0000313|EMBL:RAR45523.1, RC ECO:0000313|Proteomes:UP000249305}; RA Chemao El Fihri M.W., Manni A., Laamarti M., Kartti S., Alouane T., RA Lahlou L., Benhrif O., Temsamani L., El Jamali J.E., Lemnouar A., RA Ibrahimi A., Filali-Maltouf A.; RT "Whole genome sequencing of Moroccan desert bacteria."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS CC can inadvertently accommodate and process structurally similar amino CC acids such as valine, to avoid such errors it has two additional CC distinct tRNA(Ile)-dependent editing activities. One activity is CC designated as 'pretransfer' editing and involves the hydrolysis of CC activated Val-AMP. The other activity is designated 'posttransfer' CC editing and involves deacylation of mischarged Val-tRNA(Ile). CC {ECO:0000256|ARBA:ARBA00025217, ECO:0000256|HAMAP-Rule:MF_02003}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L- CC isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, CC Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, CC ChEBI:CHEBI:456215; EC=6.1.1.5; CC Evidence={ECO:0000256|ARBA:ARBA00000114, ECO:0000256|HAMAP- CC Rule:MF_02003}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02003}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02003}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003}. CC -!- DOMAIN: IleRS has two distinct active sites: one for aminoacylation and CC one for editing. The misactivated valine is translocated from the CC active site to the editing site, which sterically excludes the CC correctly activated isoleucine. The single editing site contains two CC valyl binding pockets, one specific for each substrate (Val-AMP or Val- CC tRNA(Ile)). {ECO:0000256|HAMAP-Rule:MF_02003}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC IleS type 2 subfamily. {ECO:0000256|ARBA:ARBA00007078, CC ECO:0000256|HAMAP-Rule:MF_02003}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RAR45523.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QLYT01000008; RAR45523.1; -; Genomic_DNA. DR EnsemblBacteria; RAR45523; RAR45523; DP091_04350. DR Proteomes; UP000249305; Unassembled WGS sequence. 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-UniRule. DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR033709; Anticodon_Ile_ABEc. DR InterPro; IPR002301; Ile-tRNA-ligase. DR InterPro; IPR023586; Ile-tRNA-ligase_type2. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR PANTHER; PTHR42780; PTHR42780; 1. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR PRINTS; PR00984; TRNASYNTHILE. DR SUPFAM; SSF47323; SSF47323; 2. 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 {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_02003}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_02003}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02003}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02003}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02003}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_02003}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_02003}; Zinc {ECO:0000256|HAMAP-Rule:MF_02003}. FT DOMAIN 17..621 FT /note="tRNA-synt_1" FT /evidence="ECO:0000259|Pfam:PF00133" FT DOMAIN 676..821 FT /note="Anticodon_1" FT /evidence="ECO:0000259|Pfam:PF08264" FT MOTIF 47..57 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003" FT MOTIF 590..594 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003" FT BINDING 593 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003" SQ SEQUENCE 1029 AA; 116112 MW; 073D03DD8978EE3E CRC64; MNRVDVKEKA RARELRILNK WNEENTFKKS IELRAGKPNY VFYEGPPTAN GAPHIGHVLG RVIKDFVGRY QTMKGYHVVR KAGWDTHGLP VELGVEKQLG ISGKQEIENY GVEAFIKKCK ASVFEYEHKW RELTEAIAYW TDLDHPYITL ENNYIESVWN ILATIHDKGL LYRGHRVSPY CPCCQTTLSS HEVAQGYEDV KDLSATAKFK LHDSGEYVLA WTTTPWTLPS HVALAVNPDM DYARVEQEDG IYIVAKNLVE DVMKGDFTVL STLKGSELVG KTYDPPFPYV KAEKANLIVG ASFVTDASGT GIVHMAPAHG EDDYRVCREN GISFVSVVNG QGRYTDEVTD FAGRFVKDCD LDIVKALSEK GLLYSKEKYE HSYPFCWRCK SPLLYYAMES WFIETTAVKD QLIANNNEVT WYPGHVREGR FGKFLEDLVD WNISRNRYWG TPLNVWVCDS CEGQFSPHSI AELRSNAVGE VAEDLELHKP YVDEVKVKCP HCEGGVMERT SEVIDVWFDS GSMPYAQYHY PFEDKEKFEQ QYPADMICEG IDQTRGWFYS LLAVSTLFTG KAPYKAVMAT GHILDENGQK MSKSKGNVID PWEIIEEYGT DAFRWALLAD SAPWNSKRFS KGIVGEAKSK VVDTLVNTHA FLTLYAGIDG YDPKEHHFQG SNHKLDRWIL SRLNSLIQVV DKGLAVNDFL NAAKAIEAYV DELSNWYIRR SRDRFWGSGL GEDKLAAYGT LTHVLLTLSK LMAPFTPMLS EDIFVNLGGG ESVHLADFPQ ADEALIDKAL EQDMETARQI VELARNVRNE TGIKTRQPLS ELIVSMDREF DLAGYEDIIK DEINVKAIEV ETSDSGFVDF MLKMNLKVAG KKYGKNIGFL QGFLKGMSSD ETRKVVQTGG VNVTSPEGEE LQITSEELLV EKKAKEGFAS ASGYGLTVAL NTDITRELEQ EGWVREVVRA VQDTRKKLDL PIEKRVNLIL DTDEELKVAI TAFEDVLREN VLVNDLQFGQ SEDMERVELG GKTIGIHIA //