ID J1GQ67_9FLAO Unreviewed; 1135 AA.
AC J1GQ67;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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 ECO:0000313|EMBL:EJF35043.1};
GN ORFNames=HMPREF1320_1248 {ECO:0000313|EMBL:EJF35043.1};
OS Capnocytophaga sp. oral taxon 335 str. F0486.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1125720 {ECO:0000313|EMBL:EJF35043.1, ECO:0000313|Proteomes:UP000004158};
RN [1] {ECO:0000313|EMBL:EJF35043.1, ECO:0000313|Proteomes:UP000004158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0486 {ECO:0000313|EMBL:EJF35043.1,
RC ECO:0000313|Proteomes:UP000004158};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (MAY-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_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|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:EJF35043.1}.
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DR EMBL; AKFR01000037; EJF35043.1; -; Genomic_DNA.
DR RefSeq; WP_009418562.1; NZ_AKFR01000037.1.
DR AlphaFoldDB; J1GQ67; -.
DR PATRIC; fig|1125720.3.peg.2031; -.
DR Proteomes; UP000004158; 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; cd00818; IleRS_core; 1.
DR Gene3D; 3.30.720.200; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 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 NCBIfam; TIGR00392; ileS; 1.
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; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 2.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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}; Cytoplasm {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 18..721
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 770..922
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 683..687
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 686
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1135 AA; 128608 MW; 88FFF933C9DD5F0D CRC64;
MKFNEYKHLD LTKIAEEILA FWKAANIFEQ SIASRDGAIP FVFFEGPPSA NGVPGIHHVM
ARSIKDIFCR YKTQKGFQVK RKAGWDTHGL PVELGVEKEL GITKEDIGKK ISVEDYNKAC
KEAVMRYTDI WNDLTEKIGY WVDMEDPYIT YKPKYMESVW WLLKQLYNKG LLYKGYTIQP
YSPKAGTGLS SHELNQPGCY RDVSDTTVVA QFKVKALATT ATKALGDPTE PIHILAWTTT
PWTLPSNTAL AVGKEIEYVL VRTYNQYTFE PITIIIGKPL LAKQFSKKFV EGDAQALAAY
TPESKTIPYQ VLGECKGADL VGTTYEQLIP WCVPAENADQ AFRVIAGDFV TTDDGTGIVH
IAPTFGADDA RVAKEYGVPP MLVKDAHGNL IPLIDLQGKF ITGHNIPEAF AGKYIKNEYY
DAGQAPEKSW DVSLAILLKE ENKAFKVEKY VHSYPHCWRT DKPVLYYPLD SWFVRVTDFK
ERMFDLNETI NWKPKATGEG RFGNWLKNAN DWNLSRSRYW GIPLPIWRTA DKQEEICIGS
VEELKAEIQK AIVAGVMTAD PYKDFVVGDK SESNYDKVDL HKNIVDNIVL VSPSGKPMHR
ETDLIDVWFD SGSMPYAQWH YPFENKEFID NHTAYPADFI AEGVDQTRGW FYTLHAIGTS
VFNSVAYKNV VSNGLVLDKN GQKMSKRLGN AVDPFTTIAE YGADATRWYM ISNANPWDNL
KFDLEGVAEV RRKFFGTLYN TYSFFALYAN TDSFTYAEAD IPLAERPEID HWILSELNTL
IKEVDALYAD YEPTRATRAI SDFVQENLSN WYVRLSRRRF WKGEYETDKI AAYQTLYTCL
ITIAKLMAPV APFYADRLYK DLVSVTGKEN KESVHLTDFP VANESYIDKS LESKMQKAQT
ISSLVLSLRK KESIKVRQPL QKIMIPIANA TERAEIEAVA NLIKHEVNVK EIELLEDASG
ILVKQIKPNF KTLGPKFGKD MKAIATAVQE FGQQEIAQFE KAQTYSLQLP DKTVTLSLDD
VEISTQDIEG WLVATAGSLL VALDIHITPE LRQEGIAREL VNRIQNIRKD NDYDITDRIQ
IRLQAHTALQ EAVTANEAYI KNETLTDSIS FVDSLPEGEE IAFDEVTTRI VVSRS
//
