ID A0A0G1XHD5_9BACT Unreviewed; 1153 AA.
AC A0A0G1XHD5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=UY24_C0019G0004 {ECO:0000313|EMBL:KKU93730.1};
OS Parcubacteria group bacterium GW2011_GWA1_48_11b.
OC Bacteria.
OX NCBI_TaxID=1618795 {ECO:0000313|EMBL:KKU93730.1, ECO:0000313|Proteomes:UP000034426};
RN [1] {ECO:0000313|EMBL:KKU93730.1, ECO:0000313|Proteomes:UP000034426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKU93730.1}.
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DR EMBL; LCPG01000019; KKU93730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1XHD5; -.
DR PATRIC; fig|1618795.3.peg.422; -.
DR Proteomes; UP000034426; 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 CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.620; HUPs; 3.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
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:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF19302; DUF5915; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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 12..482
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 705..824
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 877..1018
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 593..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 794..798
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 797
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1153 AA; 132629 MW; D244136D2F56A338 CRC64;
MADFNFAKIE EKILNFWKER DIFKKSLEAR RKAKRFVFWE GPPTANGHPH MGHFEGRVFK
DLFCRYKTMR GFFVLRKAGW DTHGLPVEIE VEKELGFKNK KDIEEYGIAK FNRKCRENIW
KYKAEWEEMT QKMGFWLDLG NPYITYETKY MESVWQILKT IWDKKLLYPA HKVVHFCTRC
GTPLAAHEVA QGYRRTTDRS VFVKFKVKSE KFKGAYILAW TTTPWTLPGN VALAVGNDIN
YVLVEWNEEK FILAKDLIEK VFSQNSKFKV QNSFKGSDLI GLEYEPLFDI PQLKSETSYK
IYAADFVSTE EGTGVVHTAV MYGEDDYNLG TKLGLLKVHT VDETGKFNSA AGKELEGLYV
KSNATEEKII KSLEEKGLLL KIEAYEHDYP FCWRCGTPLI YYAKDSWFIK ISAVKDELLK
NNEKINWFPG HIKEGRFGQW LKEGKDWALS RERYWGTPLP VWKCEKCGRY EIVGSVKDLE
KKALGSGNTY LILRHGLTAR REGEGKNIVA SILEKDKYPL LPEGRAQIEK IAAVLEQAGG
ADEIYASPFL RTKETAEIVG KILHKTVKID IRLAEFKHGP ACEGKEHVLC PARETRRQNL
DEKDPGGESR NDVRERVVDF MNEMESRHQK KKILIVSHGD PLWLLGATAG GWKGDEILKD
KADPAHWYPR LAELKEIPWK KIPRDGLGEL DLHRPFADGI VLKCSNCKAK MKKIPDLIDA
WFDSGAMPYA QWHWPFENKK LFKEQFPADF IVEGVDQTRG WFYTLLAIST LLGNGAPYKT
VMSLGHVLDE KGQKLSKSKG NYVLPRDLMD KYGADAARWY FYTVNSPGDS KLFAEKELRA
QLTGPLSTLQ NCLKFYELYA DVNYQLSIIN YQLSVLDKWL LSKLNGLILE VGGKLDRYDV
TTAARAIEKF VAEDFSNWWL RRSRKRKESL PLLRAALLEI AKLCAPFIPF TAEEVHMRLH
AGTAVGTESI HLHDWPKANK KLINLKLEEE MSGVRDVVAA GLAVRKEKQI RVRQPLRAVK
INKAKKFGSG LEDLIKEELN VKKVLYDAKQ KEAVLLDLEL DQALRAEGYA REMMRQIQDM
RKEAKYKLNQ RVFVQWHSDD AELSAAINEW AENIKTETLL REFANGPRDT KNHDIQKETD
LAPGKKIWIG IGK
//
