ID A0A345NLI8_9MICO Unreviewed; 1133 AA.
AC A0A345NLI8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=DV701_06925 {ECO:0000313|EMBL:AXH95896.1};
OS Ornithinimicrobium avium.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Ornithinimicrobium.
OX NCBI_TaxID=2283195 {ECO:0000313|EMBL:AXH95896.1, ECO:0000313|Proteomes:UP000253790};
RN [1] {ECO:0000313|EMBL:AXH95896.1, ECO:0000313|Proteomes:UP000253790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMA3305 {ECO:0000313|EMBL:AXH95896.1,
RC ECO:0000313|Proteomes:UP000253790};
RA Bae J.-W.;
RT "Complete genome sequencing of Ornithinimicrobium sp. AMA3305.";
RL Submitted (JUL-2018) 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; CP031229; AXH95896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345NLI8; -.
DR KEGG; orn:DV701_06925; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000253790; 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}; Reference proteome {ECO:0000313|Proteomes:UP000253790};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 26..694
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 745..882
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1084..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 60..70
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 660..664
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 663
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1133 AA; 125926 MW; 6DFB59EABC253B72 CRC64;
MAYPLTSTSG AALTSSPRFP EIEEAVLAYW KEHGTFVRSV EQRPAGQDGD NEYVFYDGPP
FANGLPHYGH LLTGYVKDVV PRYQTMRGRR VERRFGWDTH GLPAELEAMA QLGIKTKEEI
LELGIEAFNA KCRESVLQYT SDWEDYVTRQ ARWVDFEGDY KTLNVGYMES VLWAFKSLYD
KGLVYEGFRV LPYCWNDQTP LSNHELRMDD EVYQVRQDPA VTVGVRLLPG DSPDPVLDGA
LALVWTTTPW TLPANLAVMV GEDIEYVVVR APLPGAGEDA EPARYLIAKE RLTAYSSELG
GEDAAPEVLA TYAGKELAGR SYVPPFTYYQ GWQRAHRVVV AEFVTTTDGT GLVHTAGAFG
EDDKVVTDRE GIEPVMPVGP DGAFLHPVDE YAGMLVFDAN APIQEHLRAA TLNQLPRTDE
HPVLLDQGAV AAGTVLLRRE TYAHSYPHCW RCRQPLIYKA VSSWFVEVTK LKDDMLATNE
QITWVPEHVK HGQFGKWLEN ARDWSISRNR FWGSPIPVWR SDDPEHPRID VYGSLAQLEA
DFGQLPRDRE GNVDLHRPFV DELTRPNPDD PSGRSTMRRV EDVLDVWFDS GSMSYAQVHY
PFENAEWFEH HFPADFIVEY IGQTRGWFYT LHILATALFD RPAFQNCISH GIVLGNDGQK
MSKSLRNYPD VREVFARDGA DAMRWFLMSS PILRGGNLVV TEQGIRDGVR QTMIPLWNAW
YFYGLYANAA GYEASWSTGS THELDRYVLA KTRDFVDTAQ GAYDRNDIAT AADAIREFVD
VLTNWYIRRS RDRFWAEDHE AFDTLYTVLE VTCRVAAPLL PLLTEEVWRG LTGGESVHLT
DWPDAEDLPA DADLVAAMDT VREVCSAALA LRKGEGLRVR LPLASLTVVT PHAEMLEGRP
ALADLVRDEV NVRELVLLDP AALGAEDEVQ VEQRLTVNAR AAGPRLGRDV QAAIRGSKTG
DWSVAEDGTV TSGGLQLLEG EYALETVVSD EHGASRATAM LRGQGGGFVV LDTEVTEDLA
REGLARDLVR GVQGARKEAG LDITDRISLT VVGDDEVWDA ATAHQRLVMD ETLAVQFGAA
GAGTPLPRAK HHGLGGGSDP DGGTQPRPTA YTTTADLGGG HEVELMIVKV EAR
//
