ID A0A0M4QJ56_9MICC Unreviewed; 1090 AA.
AC A0A0M4QJ56;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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:ALE94092.1};
GN ORFNames=AOC05_08015 {ECO:0000313|EMBL:ALE94092.1};
OS Arthrobacter alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=656366 {ECO:0000313|EMBL:ALE94092.1, ECO:0000313|Proteomes:UP000062833};
RN [1] {ECO:0000313|Proteomes:UP000062833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R3.8 {ECO:0000313|Proteomes:UP000062833};
RA See-Too W.S., Chan K.G.;
RT "Complete genome of Arthrobacter alpinus strain R3.8.";
RL Submitted (SEP-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}.
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DR EMBL; CP012677; ALE94092.1; -; Genomic_DNA.
DR RefSeq; WP_062009531.1; NZ_CP012677.1.
DR AlphaFoldDB; A0A0M4QJ56; -.
DR KEGG; aaq:AOC05_08015; -.
DR PATRIC; fig|656366.3.peg.1710; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000062833; 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; 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:UP000062833};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 33..690
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 746..885
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 67..77
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 656..660
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1090 AA; 121045 MW; 71025B28C14301A6 CRC64;
MTHFPKATAA TGLHADSHHV PASVSFPKVE ELVLKYWAED DTFQASIDAR DAGEDGSNEF
VFYDGPPFAN GLPHYGHLLT GYAKDLVARY QTQRGRRVER RFGWDTHGLP AELEAMKQLG
MTDKAQIEAM GIDKFNDACR ASVMKYAGEW QEYVTRQARW VDFKHDYKTL NVEYMESVLW
AFKQLHTKGL TYNGYRVLPY CWKDETPLSN HELRMDEDVY KDRQDQTVTV TFPILAGESA
LSQELAGVAA IAWTTTPWTL PTNQALAVGP QVSYAVVPVG PHGTTAGAGK FLLAADLVGA
YAKDLGYDDA AAATSAVTAS YVGAELEGLK YEPLWDYFAD DEKYGTAKSW QFLLADYVTT
TDGTGIVHQA PAYGEEDQKV CEQYGIPVVL SVDEGANFLP LFAQGPLSEI AGVQVFDANK
SITRVLKDAG RLVRQASYVH SYPHCWRCRT PLIYRAVSSW YVEVTAFKDR MVELNQDINW
IPGNVKDGQF GKWLANARDW SISRNRYWGS PIPVWQSDDP EYPRTDVYGS LAEMAADFGR
LPVNNDGEVD LHRPFIDALT RPNPDDPTGK STMRRVEDVL DVWFDSGSMP YAQVHYPFEN
QDWFDTHNPA DFIVEYIGQT RGWFYMLHIL STALFDRPAF RNVISHGIVL GSDGQKMSKS
LRNYPDVSEV LDRDGSDAMR WFLMSSPILR GGNLVVTEQG IRDGVRQVIL PLWNVYSFFT
LYANTANNGQ GYDAKLRFDG YTDTMDQYLL ANTGDLVREL TAKLDDYDVS GACDSLRNYL
DMLTNWYVRR SRGRFFDENA DAFDALYTAL ETVCRVAAPL LPLVTEEIWR GLTGGRSVHL
TDWPNAELFV SNAALVEQMD KIQQICSTGS SLRKAAKLRV RLPLQELTVV APNAALLNDG
AAIVAEELNI RTVRFVDASD ASPEEFGITS KLVVNARAAG PRLGKNVQLA IKGSKSGDWS
ITDGVVTAGG LALEPSEYTL ETMVTEASDG GQSAVAMLPH GGFVVLDTEL TPELEAEGAA
RDMVRAIQQA RKDAGLNVSD RIRTIISAPQ DVVDALHANA ELVKKETLTL KLELIPGDVE
TTITVERTIA
//
