ID A0A328WGZ0_PAELA Unreviewed; 1029 AA. AC A0A328WGZ0; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 08-MAY-2019, entry version 5. 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; OC 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 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). {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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_02003, ECO:0000256|SAAS:SAAS01125826}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC 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 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)). {ECO:0000256|HAMAP- CC Rule:MF_02003}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. IleS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02003}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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; -; 1. DR Gene3D; 3.90.740.10; -; 1. 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 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|HAMAP-Rule:MF_02003, KW ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470441}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02003, KW ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470429}; KW Complete proteome {ECO:0000313|Proteomes:UP000249305}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02003, KW ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00106025, KW ECO:0000313|EMBL:RAR45523.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02003}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02003, KW ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470402}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02003, KW ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470368}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}. FT DOMAIN 17 621 tRNA-synt_1. {ECO:0000259|Pfam:PF00133}. FT DOMAIN 676 821 Anticodon_1. {ECO:0000259|Pfam:PF08264}. FT MOTIF 47 57 "HIGH" region. {ECO:0000256|HAMAP-Rule: FT MF_02003}. FT MOTIF 590 594 "KMSKS" region. {ECO:0000256|HAMAP-Rule: FT MF_02003}. FT BINDING 593 593 ATP. {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 //