ID A0A829BJE6_STREE Unreviewed; 930 AA. AC A0A829BJE6; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 19-JAN-2022, entry version 2. DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02002}; DE EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02002}; DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02002}; DE Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02002}; GN Name=ileS {ECO:0000256|HAMAP-Rule:MF_02002}; GN ORFNames=PCS70012_00254 {ECO:0000313|EMBL:ELU64171.1}; OS Streptococcus pneumoniae PCS70012. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1159085 {ECO:0000313|EMBL:ELU64171.1, ECO:0000313|Proteomes:UP000011904}; RN [1] {ECO:0000313|EMBL:ELU64171.1, ECO:0000313|Proteomes:UP000011904} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCS70012 {ECO:0000313|EMBL:ELU64171.1, RC ECO:0000313|Proteomes:UP000011904}; RA Williams T., Loman N., Ebruke C., Qin X., Clifton S., Fulton L., Fulton B., RA Courtney L., Hall O., Fronick C., Harrison M., Strong C., Farmer C., RA Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A., Yan L., RA Wang C., Shah N., Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., RA Warren W., Chinwalla A., Murphy D., Keitel W., Musher D., Sodergren E., RA Mardis E.R., Wilson R.K., Adegbola R.A., Pallen M., Weinstock G.M., RA Antonio M.; RL Submitted (MAR-2012) 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_02002}. 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_02002}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02002}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_02002}; CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP- CC Rule:MF_02002}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02002}. 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_02002}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC IleS type 1 subfamily. {ECO:0000256|ARBA:ARBA00006887, CC ECO:0000256|HAMAP-Rule:MF_02002}. 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:ELU64171.1}. 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; AKQY01000001; ELU64171.1; -; Genomic_DNA. DR RefSeq; WP_001844534.1; NZ_KB371258.1. DR Proteomes; UP000011904; Unassembled WGS sequence. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1. 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; IPR033708; Anticodon_Ile_BEm. DR InterPro; IPR002301; Ile-tRNA-ligase. DR InterPro; IPR023585; Ile-tRNA-ligase_type1. 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 InterPro; IPR010663; Znf_FPG/IleRS. 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; SSF47323; 1. 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_02002}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_02002}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02002}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02002}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02002}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_02002}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_02002}; Zinc {ECO:0000256|HAMAP-Rule:MF_02002}. FT DOMAIN 27..634 FT /note="tRNA-synt_1" FT /evidence="ECO:0000259|Pfam:PF00133" FT DOMAIN 678..831 FT /note="Anticodon_1" FT /evidence="ECO:0000259|Pfam:PF08264" FT DOMAIN 885..913 FT /note="zf-FPG_IleRS" FT /evidence="ECO:0000259|Pfam:PF06827" FT MOTIF 57..67 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002" FT MOTIF 595..599 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002" FT METAL 888 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002" FT METAL 891 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002" FT METAL 908 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002" FT METAL 911 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002" FT BINDING 554 FT /note="Aminoacyl-adenylate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002" FT BINDING 598 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002" SQ SEQUENCE 930 AA; 105162 MW; 21E298FD06307DE2 CRC64; MKLKDTLNLG KTAFPMRAGL PTKEPVWQKE WEDAKLYQRR QELNEGKPHF VLHDGPPYAN GNIHVGHAMN HISKDIIIRS KSMSGFNSPY IPGWDTHGLP IEQVLAKQGV KRKEMNLVEY LKLCREYALS QVYKQRDDFK RLGMSGDWEN LYVTLTPDYE AAQIRVFGEM ANKGYIYRGA KPVYWSWSSE SALAEAEIEY HDLVSTSLYY ANKVKDGKGV LDTDTYIVVW TTTPFTITAS RGLTVGADID YVLVQPAGEV RKFVVAAELL TSLSEKFGWA DVQVLATYRG QELNHIVTEH PWDTAVDELV ILGDHVTTDS GTGIVHTAPG FGEDDYNVGI ANGLEVAVTV DERGIMMKNA GPEFEGQFYD KVVPTVIEKL GNLLLAQEEI SHSYPFDWRT KKPIIWRAVP QWFASVSKFR QEILDAIDKV KFHTEWGKVR LYNMIRDRGD WVISRQRAWG VPLPIFYAED GTAIMTAETI EHVAQLFEVH GSSIWWERDA KDLLPEGFTH PGSPNGEFKK ETDIMDVWFD SGSSWNGVLV NRPNLTYPAD LYLEGSDQYR GWFNSSLITS VANHGVAPYK QILSQGFTLD GKGEKMSKSL GNTIAPSDVE KQFGAEILRL WVTSVDSSND VRISMDILSQ VSETYRKIRN TLRFLIANTS DFNPAQDAVA YEELRSVDKY MTIRFNQLVK TIRDAYANFE FLTIYKALVN FINVDLSAFY LDFAKDVVYI EGAKSLERRQ MQTVFYDILV KITKLLTPIL PHTAEEIWSY LEFEAEDFVQ LSELPEAQTF ANQEEILDTW AAFMDFRGQA QKALEEARNA KVIGKSLEAH LTVYPNEVVK TLLEAVNSNV AQLLIVSELT IAEGPAPEAA LSFEDVAFTV ERAAGEVCDR CRRIDPTTAE RSYQAVICDH CASIVEENFA EAVAEGFEEK //