ID A0A2T3WD28_9DEIO Unreviewed; 1057 AA.
AC A0A2T3WD28;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=C8263_01950 {ECO:0000313|EMBL:PTA69799.1};
OS Deinococcus arcticus.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2136176 {ECO:0000313|EMBL:PTA69799.1, ECO:0000313|Proteomes:UP000240317};
RN [1] {ECO:0000313|EMBL:PTA69799.1, ECO:0000313|Proteomes:UP000240317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OD32 {ECO:0000313|EMBL:PTA69799.1,
RC ECO:0000313|Proteomes:UP000240317};
RA Wang X.-P., Du Z.-J.;
RT "Draft genome of Deinococcus sp. OD32.";
RL Submitted (MAR-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|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:PTA69799.1}.
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DR EMBL; PYSV01000001; PTA69799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3WD28; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000240317; 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; 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.
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}; Cytoplasm {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 20..633
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 689..840
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 50..60
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 603..607
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1057 AA; 119231 MW; 41826EB810312BD3 CRC64;
MTTFKPVPQN PNFPAMEGDI LAFWKEGRIF ERSLEQTKGG PVFTFYEGPP TANGQPGVHH
VQARSFKDLF PRFRTMQGHH VPRKAGWDTH GLPVELGVEK KLGLNSKREV EAYGIDRFNA
ECRASVFEYE AEWRRFTERM GYWVDLDDAY LTLHKDYIES VWWSVKGLDE KGLLYKGFRV
APYCPKDGTT LSNAEVSEGY RDIQDPSVYV PFRLKDPARL DLPEGAAFLV WTTTPWTLPY
NVGVAIHPDF TYVAAKDKEG AVLILAASLK NEVLGEAAEV VKTFVGRELD RVAYEPLFTE
AYEAEGEGKP VWLSGLDTYV SDSDGTGIVH TAPAFGEDDM RLARNYGFPV VVGVDSEGKH
RFGPWKGVFF RDANTEIVRD LRARGLMWRE KNFLHAYPHC WRCGTPLMYY ATESWYLNNT
RLKARLIELN QTIDWHPPHI RNGRYGGWLE NLIDWNVSRS RYWGTPLPVW EAEDGEYRVV
GSYAELSELS GRPEVTGPDF DPHRPFVDDI TFEVSGKTFR RVPYVMDVWY DSGAMPFAQH
HYPFENREKF EAGGFPADFI AEAIDQTRGW FNSLHQIGTM VFDSVAYKSV ICSGHILDEK
GAKMSKSKGN IVSPWDVFEL YGADAARWYM YVSAPPELSR RFGMNLVGEA FRSYFLTLWN
TYSFFVLYAN LDRPDLGAAA PVAERPEVDR WLVAKVQALI AAVTERLENY DPTGASRALQ
DFVVEDLSNW YVRRNRRRFW GEGGQVDHNA YATLHFALVT VTTLTAPFTP FLAETLYGNL
VRSLDPGAPD SVHLTAWPVV DEALSAPTLV NEMDAVLRVV SLGRAVRGQT GLRQRQPLPK
VMVRARTAEQ TAALGRFAEQ IKEELNVKEV ELMDQFTELV RYQLRPNLPV LGKKFGKAVP
QVRAALGAAD ASEVARFVRD SKQFEVVAPT GERFELGPDE VLVDAQSPEG FAAQEEAGYL
VAFDTTLTRE LELEGLARDL VRGVQDARKK AGFEVQDRIA LHLELSGDAR EAAEAWQEYL
MSETLAETLV FGVADGFAAE VEGGTAYLEK LEVVSHN
//