ID E7NEC9_9ACTO Unreviewed; 1119 AA.
AC E7NEC9;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 75.
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:EFW25477.1};
GN ORFNames=FBF36_08730 {ECO:0000313|EMBL:QCT33526.1}, HMPREF9057_03177
GN {ECO:0000313|EMBL:EFW25477.1};
OS Actinomyces sp. oral taxon 171 str. F0337.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=706439 {ECO:0000313|EMBL:EFW25477.1, ECO:0000313|Proteomes:UP000005722};
RN [1] {ECO:0000313|EMBL:EFW25477.1, ECO:0000313|Proteomes:UP000005722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0337 {ECO:0000313|EMBL:EFW25477.1,
RC ECO:0000313|Proteomes:UP000005722};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCT33526.1, ECO:0000313|Proteomes:UP000310751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0337 {ECO:0000313|EMBL:QCT33526.1,
RC ECO:0000313|Proteomes:UP000310751};
RA Collins A.J., Murugkar P., Chen T., Dewhirst F.E.;
RT "Saccharibacteria TM7 and host bacteria genomes.";
RL Submitted (APR-2019) 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|ARBA:ARBA00007078,
CC ECO:0000256|HAMAP-Rule:MF_02003}.
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DR EMBL; AECW01000575; EFW25477.1; -; Genomic_DNA.
DR EMBL; CP040005; QCT33526.1; -; Genomic_DNA.
DR RefSeq; WP_009398779.1; NZ_GL637953.1.
DR AlphaFoldDB; E7NEC9; -.
DR SMR; E7NEC9; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_11; -.
DR Proteomes; UP000005722; Unassembled WGS sequence.
DR Proteomes; UP000310751; Chromosome.
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; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
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}; Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 44..700
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 764..903
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 75..85
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 666..670
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 669
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1119 AA; 124896 MW; 9A48F227159711AB CRC64;
MAEKMADSTT AGGSEPTGAA FYPLHRPGEQ IDPSPSFPAI EEDVLAYWKA DGTFQASIDN
RGEPCDEFVF YDGPPFANGL PHYGHLLTGY VKDAVGRYQT QRGKRVERRF GWDTHGLPAE
LEAQRLLGID DVTEITRPGG IGIEKFNEEC RSSVLRYTKE WEDYVTRQAR WVDFDNDYKT
LDPDYMESVL WAFKQLWDKG LAYQGYRVLP YCWHDRTPLS NHELKMDDDV YQDRQDNTVT
VGLRLEEPLR QGAERPELVL IWTTTPWTLP SNLAIAVGPD VEYVTVHVDE DLDSPVAGQD
VVMARDLLGA YARELGEEPQ VVSTCTGADL VGRRYHPIFD YFDDAAHRAE GAAPGPKAWQ
IIAADFVTTS DGTGLVHMAS AFGEDDMIAC TEAGIETVVP VDDGGRLTEE VSDYAGLQVF
EANKPIVADL RDGTGPLARR NENQRAVLVR QASYVHSYPH CWRCRKPLIY KAVSSWFVRV
SAIRDRMVEL NQDIDWYPGH IKDGIFGKWL ANARDWSISR NRFWGAPIPV WVSDNPDYPR
TDVYGSYAEL ERDFGVKVTD LHRPFIDTLV RPNPDDPTGT SMMRRIPDVL DCWFESGSMP
FAQVHYPFEN VEWFESHYPG DFIVEYIGQT RGWFYTLHVL ATALFDRPAF TSCVSHGILL
GNDGAKMSKS LRNYPDVSMV FDRDGADAMR WFLLSAPVMR GGNLVVTDKA IRDTVRQVVL
PLWNTWYFFA LYAGQAGQSG YVTDGVDLSD ASLFAKHGGL HVMDRYVLAR TKDLAETVAA
QMDGYDITGA CATIRDFLDV LTNWYLRTSR QRFTDGETAA FDTLATVLRV LTEVMAPLAP
LVSEEIWRGL TGGRSVHLTD WPVLPNHVAN AELVTAMDEA RAAVSAALSL RKAEKLRVRQ
PLRSLTIATA DPAGLAPFRE LVAEEVNVKE VRVLDAESAG YEARTDLALN PRAFSPEVRK
LTSRLFAAVK AGQWELTEDG DVRFNDVLLD GTPVVLEAED SAFTLTTRIE VDDDSLAATM
LPSGAFVVLE TALDDALEAE GWARDLVRLV QDERKAAGLH VGDRIRMELR VPEDKGAWTG
AHLDLIKREV GCVDASVVAD PAAKDPTATV EKVSETTDR
//
