ID A0A0A0BY00_9CELL Unreviewed; 1079 AA.
AC A0A0A0BY00;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
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:KGM12840.1};
GN ORFNames=N869_01520 {ECO:0000313|EMBL:KGM12840.1};
OS Cellulomonas bogoriensis 69B4 = DSM 16987.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM12840.1, ECO:0000313|Proteomes:UP000054314};
RN [1] {ECO:0000313|EMBL:KGM12840.1, ECO:0000313|Proteomes:UP000054314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=69B4 {ECO:0000313|EMBL:KGM12840.1,
RC ECO:0000313|Proteomes:UP000054314};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas bogoriensis 69B4.";
RL Submitted (AUG-2013) 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:KGM12840.1}.
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DR EMBL; AXCZ01000090; KGM12840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0BY00; -.
DR Proteomes; UP000054314; 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}; Reference proteome {ECO:0000313|Proteomes:UP000054314};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 29..672
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 731..871
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 64..74
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 638..642
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1079 AA; 119916 MW; 1844E37F1830D537 CRC64;
MVYPLHRTTD VGTPAPVPAS PDLPDVERQV LDHWQADGTF QASVDQRPAG AQGENEFVFY
DGPPFANGLP HYGHLLTGYV KDVVGRYRTQ RGRRVERRFG WDTHGLPAEL EAERVLGITD
KAQIDQMGIA AFNEACRTSV LRYTHEWQEY VTRQARWVDF DNDYKTLDVT YMESVLWAFK
QLHDKGLAYE GYRVLPYCWR DETPLSNHEL RMDDDVYAQR QDPALTIGVR LETGELALIW
TTTPWTLPSN LAIAVGPDID YVVVVPQEGS ALAGERLVLA AARLWSYARE IGEEPTVLET
LTGAELAGRR YTPPFGYFEG RPHAHRVLLG DFVTTEDGTG LVHLAPAFGE DDMVVCDAAG
IEPVVPVDSK GRFTAEVRDY AGQQVLEANA QVIADLKSGD GPLSAVAEAQ RAVVVRHETY
DHAYPHCWRC RNPLIYKAMS SWFVRVSEFR DRMVELNQQI TWVPEHIKDG QFGKWLSGAR
DWSISRNRYF GTPLPVWVSD DPAHPRTDVY GSLAELEADF GRVPRNEAGE PDLHRPYIDE
LTRPNPDDPT GRATMRRIPD VLDVWFDSGA MPFAQVHYPF ENSDWFEHHY PGDFITEYIG
QTRGWFYTLH VLATALFDRP AFRTSLSHGI VLGDDGRKAS KSLRNYPDPT EMWDRYGSDA
VRWTLMSSPV LRGGNLVVAE DSIRESVRQV LLPLWSTYYF FTLYAGAAAG GEGYRAQPVT
PDRAQGLPPM DRYLLARTHD LVSTVTAALD GYELAAACEA LRDHLDVLTN WYVRTQRDRF
WAEDADAFDT LWTALEVLTR VIAPLAPLLG EEVWRGLTGG RSVHLTDWPR TTDLTADDAL
VQAMDQVRQI VSAALGLRKA NGLRVRQPLR EIAVAVADPA ALEPYRDLVA TELNVKHLTL
VDLAEVGPAE LGVTSRLAVN ARALGPRIGR QVQTVIRAAK AGDWEQTPDG VAVRTPDGTV
TLQEGEYDLT TVVAEGLGAD RVAAVLRDGG VVLLDTALDD ELRAEGLARD AVRVVQDERK
AAGLQISDRI HLTLTVPAEH LDAVRTHQEM IARETLAVDV TLTAGATTGA AVTVAGGTP
//
