ID A0A917DVI1_9BACL Unreviewed; 1031 AA.
AC A0A917DVI1;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
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=ileS2 {ECO:0000313|EMBL:GGD70859.1};
GN Synonyms=ileS {ECO:0000256|HAMAP-Rule:MF_02003};
GN ORFNames=GCM10010911_30900 {ECO:0000313|EMBL:GGD70859.1};
OS Paenibacillus nasutitermitis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=1652958 {ECO:0000313|EMBL:GGD70859.1, ECO:0000313|Proteomes:UP000612456};
RN [1] {ECO:0000313|EMBL:GGD70859.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15178 {ECO:0000313|EMBL:GGD70859.1};
RX PubMed=25193709;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Walter F., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium casei LMG S-19264T (=DSM
RT 44701T), isolated from a smear-ripened cheese.";
RL Int. J. Syst. Evol. Microbiol. 189:76-77(2014).
RN [2] {ECO:0000313|EMBL:GGD70859.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15178 {ECO:0000313|EMBL:GGD70859.1};
RA Sun Q., Zhou Y.;
RL Submitted (SEP-2020) 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=tRNA(Ile) + L-isoleucine + ATP = L-isoleucyl-tRNA(Ile) + AMP +
CC diphosphate; Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, Rhea:RHEA-
CC COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, ChEBI:CHEBI:456215; EC=6.1.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00048359, ECO:0000256|HAMAP-
CC Rule:MF_02003};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|HAMAP-Rule:MF_02003};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_02003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC 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:GGD70859.1}.
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DR EMBL; BMHP01000002; GGD70859.1; -; Genomic_DNA.
DR RefSeq; WP_188992825.1; NZ_BMHP01000002.1.
DR AlphaFoldDB; A0A917DVI1; -.
DR Proteomes; UP000612456; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 3.40.50.620:FF:000063; Isoleucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000075; Isoleucine--tRNA ligase; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW 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:UP000612456};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 17..621
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 676..822
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 590..594
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1031 AA; 115963 MW; DEB1A1DAF11E59B3 CRC64;
MQRVDVKERA RARDVRVLDK WKEEQTFQQS IENRNGKPNF VFYEGPPTAN GKPHIGHVLG
RVIKDFICRY KTMSGYRVVR KAGWDTHGLP VELGVEKQLG ISGKQEIEKY GIEAFVNKCK
DSVFEYERQW RDLTEAIAYW TDMDNPYITL NNDYIESVWH ILSTIHGKGL LYRGHRVSPY
CPCCQTTLSS HEVAQGYEDV KDLSATVKFK LADSDAYVLA WTTTPWTLPA NVALAVNPKL
DYAYVRKNGE RYIVAEGLVE SVMKSDYAIE STVKGADLVG MKYEPPFRYA SLEHGHVVIS
GDFVSDTSGT GIVHIAPAHG EDDYKAARQN GVSFLNVVDN AGRYMDTVTD LAGRFVKDCD
IDIVKMLSEQ GLLFSKERYE HSYPFCWRCK SPLIYYATES WFIETTAVKD QLIANNNSVD
WYPGHIREGR FGKFLEDLVD WNISRNRYWG TPLNVWVCDS CGAQHSPGSR ADLVARSIQP
ISPDIELHKP YVDEVKLACT QCEGGVMSRT PEVIDVWFDS GSMPFAQQHY PFENKEAFTD
QYPADIICEG IDQTRGWFFS LLAVSTLYNG QAPYKAVLST GHVLDENGQK MSKSKGNVVD
PWEILDEYGA DAFRWALLAD SAPWNSKRFS RGIVGEAKSK VIDTIVNTHA FFALYASIDG
YEPAQHPYRK SAAKLDRWIV SRLNSLTHQV IRGLEANDFL NPAKAIESFV DELSNWYIRR
SRDRFWGSGL NDDKLDAYGT LHHVLLTLSR LIAPYAPILA EDIYSNLSSD MGSVHLADYP
RADEAAIDET LERDMETARQ IVELARNVRN ETGIKTRQPL SELIVALDRD FDLSAYEDII
KDEINMKSIT IASGDSGFVD FTFKLNLKAA GKKYGKLVGA IQAYLKQLTP EETHAAVQNG
MLPYTTAEGE DISLVMDELL VEKQAKAGFA SASGYQLTVA VNTDITPELE QEGLVREVIR
AVQDTRKKLD LPIEKRVHLT LDVDAELAAA LQAFESVLKE NVLLSGVDYE SIEGMERMKI
GEKEIGILIG G
//
