ID W3RP10_9BRAD Unreviewed; 1030 AA.
AC W3RP10;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
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 ECO:0000313|EMBL:ETR78492.1};
GN ORFNames=X566_13105 {ECO:0000313|EMBL:ETR78492.1};
OS Afipia sp. P52-10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1429916 {ECO:0000313|EMBL:ETR78492.1, ECO:0000313|Proteomes:UP000018975};
RN [1] {ECO:0000313|Proteomes:UP000018975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P52-10 {ECO:0000313|Proteomes:UP000018975};
RX PubMed=25874801;
RA Pickering B.S., Tyler S., Smith G., Burton L., Li M., Dallaire A.,
RA Weingartl H.;
RT "Identification of a novel afipia species isolated from an Indian flying
RT fox.";
RL PLoS ONE 10:E0121274-E0121274(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_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 -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:ETR78492.1}.
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DR EMBL; AZSJ01000003; ETR78492.1; -; Genomic_DNA.
DR RefSeq; WP_034466702.1; NZ_AZSJ01000003.1.
DR AlphaFoldDB; W3RP10; -.
DR STRING; 1429916.X566_13105; -.
DR PATRIC; fig|1429916.3.peg.2661; -.
DR eggNOG; COG0060; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000018975; 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:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 1.10.730.20; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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 NCBIfam; TIGR00392; ileS; 1.
DR PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 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_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 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}; Reference proteome {ECO:0000313|Proteomes:UP000018975}.
FT DOMAIN 44..738
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 783..933
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 74..84
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT MOTIF 700..704
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 659
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 703
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
SQ SEQUENCE 1030 AA; 115440 MW; 68A45F0B7C6F41D8 CRC64;
MTDKPQKTGQ TATEAAAHDY SKTLFLPKTD FPMRAGLPQR EPEVLKRWNE INLYEKLRSA
AKGRAKFVLH DGPPYANGNI HIGHALNKIL KDLVTRSQQM LGYDSNYVPG WDCHGLPIEW
KIEEENYRSK GKQKPDLKNP EAMIAFRREC RAYAEHWLNV QREEFKRLGV VGDWAHPYAT
MAFPAEAQIA REIMKFAQNG TLYRGSKPVM WSVVEKTALA EAEVEYEEHT SDMVWVKFPV
KDVAVRTWAV ANDPQRAALA QSEAEWEQAL AAVRQAHVVI WTTTPWTLPG NRAISYSAKI
AYGLYRVTDA PADNWAKTGD LLILADKLAA DVFKQARVTA FERTGDVTAE MLAAMVCAHP
LNGFAGGYGF DVPLLEGDHV TDDTGTGFVH TAPSHGREDF DVWTANARAL EARGVNTTIP
YTVDENGAYT EQAPGFTGKR VITDKGEKGD ANEAVIKALV EKGMLLARGR LKHQYPHSWR
SKKPVIFRNT PQWFIAMDKP IADNGTAKDG DTLRARALQA ISVTRWVPPA GQNRINGMIE
ARPDWVISRQ RAWGVPIAVF VREQGDGSVE ILKDETVNQR IAEAFMNEGA DAWYAAGARE
RFLGPKAAEG WQKVDDILDV WFDSGSTHAF VLEDRQNFPT FGNIVRKVDG GQDTVMYLEG
SDQHRGWFHS SLLESCGTRG RAPYDVVLTH GFTLDEHGRK MSKSLGNTVE PQKVIKDSGA
DILRLWVAAS DYADDQRIGP EILKNTVETY RKLRNTIRWM LGSLAHFRDE DRVKADVMPE
LERLMLHRLA EVDAVVREAY ENFDYKTVVA TLSNFMNTEL SAFYFDIRKD TLYCDPPSSL
ARKSALTVID YLFRCIVTWL APILCFTAEE AWLSRYGEAA VSVHLEPFQH VLSAWRDDAL
AKKWETIRDV RRVVTGALEL ERAAKRIGSS LEASPRVYVA DKDVFGILAG VDLSEICITS
SDEVTNADAP ADAFRLNDVP NVAVVVERAQ GKKCARSWKI LPTVGDDPDY PDVTPRDAQA
LREWKALGLI
//
