ID A0A0S9C527_9MICC Unreviewed; 1126 AA.
AC A0A0S9C527;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 47.
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:KQN88749.1};
GN ORFNames=ASE96_10055 {ECO:0000313|EMBL:KQN88749.1};
OS Arthrobacter sp. Leaf69.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN88749.1, ECO:0000313|Proteomes:UP000051467};
RN [1] {ECO:0000313|EMBL:KQN88749.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN88749.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN88749.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN88749.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KQN88749.1}.
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DR EMBL; LMLR01000011; KQN88749.1; -; Genomic_DNA.
DR RefSeq; WP_056429821.1; NZ_LMLR01000011.1.
DR AlphaFoldDB; A0A0S9C527; -.
DR SMR; A0A0S9C527; -.
DR STRING; 1736232.ASE96_10055; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000051467; 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; 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 43..714
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 770..909
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 77..87
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 680..684
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1126 AA; 124370 MW; 2634C0BC35738565 CRC64;
MTYYPKASAA PSGAGARTSD SNAASNAAGV SASVKFPEIE ERILKYWEAD GTFQASIDQR
DAGKDGSNEF VFYDGPPFAN GLPHYGHLLT GYAKDLVGRY QTQRGRRVER RFGWDTHGLP
AELEAMKQLG MTDKTQIEAM GIDKFNDACR ASVMKYADEW KSYVTRQARW VDFENDYKTL
NVEYMESVLW AFKQLHEKGL TYNGYRVLPY CWKDETPLSN HELRMDDDVY KNRQDQTVTV
TFPITAGESE LSRQLAGVQA LAWTTTPWTL PTNLALAVGP AITYVVLPAG PHGIKAASAE
APVTGSFLLA AELLGAYAKD LGYGDGAEGV AAAEAAVTSS HTGAELDGLS YEPLWDYFSD
AEKFGTENAW RFLVADYVTT TDGTGIVHQA PAYGEDDQKV CEEAGIPVVL SVDEGAKFLP
LFGHGDLAEI AGLQVFDANK PITQVLRAQG RLVRQASYEH SYPHCWRCRN PLIYRAVSSW
YVEVTKFKDR MSELNQDINW IPGNVKDGQF GKWLANARDW SISRNRYWGS PIPVWQSSDP
DYPRTDVYGS LAEIEADFGR LPLNKAGQVD LHRPFIDELT RPNPDDPRTP EEGQSVMRRV
EDVLDVWFDS GSMPYGQVHY PFQNEEWFDT HNPADFIVEY IGQTRGWFYM LHILSTALFD
RPAFRNVISH GIVLGSDGQK MSKSLRNYPD VSEVLDRDGS DAMRWFLMSS PILRGGNLVV
TEQGIRDGVR QVILPLWNVY SFFTLYTNAA DGARGYDAKL RYDGYADTLD QYLMANTGDL
VRNMTTQLDA YDISGACDEL RSYLDMLTNW YVRRSRQRFF DENVDAFDAL YTALEAVCRV
SASLLPLISE EIWRGLTGGR SVHLADWPDA DLFPANPELV EAMDRIQQIC STGSSLRKAA
NLRVRLPLQE LTVVAPGADA LDGFAAVVRD ELNLRSVRLL DAGNASPEEF GIEQKLVVNA
RAAGPRLGKN VQQAIKGSKS GDWSVSEAGV VTAGGLELEP QEYTLETVVA EAAEGEGAGP
ATRAAAVLPG GGFVVLNTEV TPELEAEGAA RDMVRAIQQA RKDAGLNVSD RIHTTVTARQ
DVVDALLANA GLVQTETLTV RLDTVAADVK EPQVSVVKTA AEKVEA
//
