ID U7DAL4_9BACT Unreviewed; 1091 AA.
AC U7DAL4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, 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 ORFNames=CALK_0237 {ECO:0000313|EMBL:ERP39072.1};
OS Chitinivibrio alkaliphilus ACht1.
OC Bacteria; Fibrobacterota; Chitinivibrionia; Chitinivibrionales;
OC Chitinivibrionaceae; Chitinivibrio.
OX NCBI_TaxID=1313304 {ECO:0000313|EMBL:ERP39072.1, ECO:0000313|Proteomes:UP000017148};
RN [1] {ECO:0000313|EMBL:ERP39072.1, ECO:0000313|Proteomes:UP000017148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACht1 {ECO:0000313|EMBL:ERP39072.1,
RC ECO:0000313|Proteomes:UP000017148};
RX PubMed=24112708;
RA Sorokin D.Y., Gumerov V.M., Rakitin A.L., Beletsky A.V., Damste J.S.,
RA Muyzer G., Mardanov A.V., Ravin N.V.;
RT "Genome analysis of Chitinivibrio alkaliphilus gen. nov., sp. nov., a novel
RT extremely haloalkaliphilic anaerobic chitinolytic bacterium from the
RT candidate phylum Termite Group 3.";
RL Environ. Microbiol. 0:0-0(2013).
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:ERP39072.1}.
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DR EMBL; ASJR01000002; ERP39072.1; -; Genomic_DNA.
DR RefSeq; WP_022635785.1; NZ_ASJR01000002.1.
DR AlphaFoldDB; U7DAL4; -.
DR STRING; 1313304.CALK_0237; -.
DR PATRIC; fig|1313304.3.peg.219; -.
DR eggNOG; COG0060; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000017148; 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; 3.40.50.620; 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; 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 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; 2.
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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000017148};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 22..512
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 530..682
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 731..881
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 54..64
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 644..648
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1091 AA; 125256 MW; B2D0C589E7D39D99 CRC64;
MAQGYFKAVD TKVNFPRVEE KILATWKKNK TFQKSLEKTR QNETEDFVFY DGPPFATGLP
HYGHLLAGTI KDIVPRYWTM RGHHVDRRFG WDTHGLPVEN EMEKEFQVSG KKEIDDMGLH
LFNEACRSIV LRYTSQWQEV VERMGRWVDF DNQYRTMDAP YMESIWWVFK EIWGKGLIYE
GFRVQPYCPR CTTPLSNFEV NEGYQDKKDI SITVKMPVKG QENTSILVWT TTPWTLPSNV
ALAVGPDIPY VKVQDGDEFF ILAEARLSAY YKNESDYTVV ETYTGRDLTG LSYTPMFPYF
AERSEKFFQV HTADFVSTED GTGIVHIAPA FGEDDFLVGK ELGLPIVCPV DEEGRYTEEV
CDYAGQFVHD ANVQIVADIK ETGRLVHKQT ITHRYPFCYR CDTPLIYKAI NTWFMQIEPL
KPNMHENNSR IHWVPGHLQK GRFGKGIEGA PDWNIARNRY WGTPIPLWRC ECGHIECVGS
LKDLHVRAGK GNEEAGKTAH KEVVSRIKKA LRDKAQSQLE KFNIDPAWAE AVGSTEISEN
DLHSHIVNAL TLSCPECENA MERTPEVLDC WFESGSMPYA QNHYPFENKE YFEKNFPANF
IAEGIDQTRG WFYTLTVLSS ALFGREAFQN VIVNGIILAE DGNKMSKRLK NYAPPQEIMD
KVGADAIRLF LINSPAVKAE NLRFSEEGVR EMARSILIPF WNAYSFFVTY ANIDSWKPTS
TEAPASDNEL DRWVISLLAY VIRDVNREME EYNLYKVVPL MVDFIDNLTN WYIRRSRRRF
WKSQNDGDKE NAYQTLYHVL VEFSKVMAPF LPFLTDAVYE NLVCGTTPDA PESVHLCDFP
RTQEKQVDED IITQMALVRN AVGIGRLLRS RYGIKNRQPL SDITVIIRDA HKRHLVADMK
HLIMDELNVK DVRLEEREES VLHISAKPNF KKLGPIFGKE MKKVGPEITA FTPEDITDLE
AGATRSVLGR DITFEDILLV RNKKEGVEVE TDGEVTLALN TEITESLARE GLVRELINRI
QNHRKESGYE VSDRITLTLS CPAPLRDAMG DFMEIIQSET LTEKLTFDDA REARETCTVE
EYSVGITSQK A
//