ID A0A1M6EKE5_9CLOT Unreviewed; 1034 AA.
AC A0A1M6EKE5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 33.
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=SAMN05444401_1597 {ECO:0000313|EMBL:SHI85748.1};
OS Clostridium amylolyticum.
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121298 {ECO:0000313|EMBL:SHI85748.1, ECO:0000313|Proteomes:UP000184080};
RN [1] {ECO:0000313|EMBL:SHI85748.1, ECO:0000313|Proteomes:UP000184080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21864 {ECO:0000313|EMBL:SHI85748.1,
RC ECO:0000313|Proteomes:UP000184080};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQZO01000002; SHI85748.1; -; Genomic_DNA.
DR RefSeq; WP_073005333.1; NZ_FQZO01000002.1.
DR AlphaFoldDB; A0A1M6EKE5; -.
DR STRING; 1121298.SAMN05444401_1597; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000184080; 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:UP000184080};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 19..618
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 675..826
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 589..593
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1034 AA; 118993 MW; 172C66D4D5C194B4 CRC64;
MYKKIDNSRS FVDMEKEIAH LWKEKDVITK NFDMNDGAEE FTFYDGPPTA NGKPHVGHVL
TRVMKDIIPR YKVMKGYHVL RKAGWDTHGL PVELEIEKKL GISGKPQIEE YGVEKFVKEC
KGSVFSYVNM WREMSEKTAY WVDMDDPYVT YHDNYIESVW WALKQMWDKD LLYKGHKIVP
YCPRCGTALS SHEVAQGYKD VKEATAFVKF KVKGEENKYI LAWTTTPWTL PSNVALAINK
SYDYVEVVQN GEHLYLAKAL LNVLDGKYEK VKEFKGEALL GMEYEQLFPF YTPEEKAFYI
VHGDFVTLSD GTGIVHIAPA YGEDDNLLGK KNGLPLINLV DAEGKFVDAV EPFKGMPVKK
ADPKILEYMK EKNLLYKSEK FTHSYPHCWR CDTALLYYPK DSWFVKMTSL RDKLLENNDK
INWYPDNVRT GRFGKFLENV IDWGISRDRY WGTPLPIWDC ECGHRECIGS RKELEEKGIN
VPEGLELHKP YIDEIKLTCP HCGKPMKRTG EVIDCWFDSG SMPFAQWHYP FENKEIFEKN
FPAQFISEAV DQTRGWFYTL LAISTAIFDK SPFENCIVLG HVLDKHGIKM SKHKGNVVDP
LDVLENQGAD ATRWHFYTAS APWLPTRFSE DDVAEAGRKF LSTLWNVYSF YVLYAEIDKF
NPLEYSDFVS DNVMDKWIMS RLNTLVKTVD EDLHSYRITQ AALAVEEFTD ELSNWYVRRN
RSRYWSETLT DDKIGAYVTL YRVLTTLVKV AAPFVPFITE EIYQNLVVAL DKDAKESIHL
CTWPSYNAEL VDEKLEAEMD MASKIVKLGR SARNGANIKN RQPLSKMLVS TKSLPAYYGD
IIKDELNIKE VQFGADLSKY VNFEIKPNLP VLGRAYGKLI PAIRAEIAKK NQMELAQKVQ
NGGTEVINVN GEEITLNSEN LLVTMQGLEG YAFSGEGEMG VVLDTTITAE LKEEGHLREI
ISKVQNMRKE SGFEVSDKIK LYAAHNDMLL EVIKKFEDFI KKETLSVEVL YNAEAEYTET
TINGEKLDLK VERK
//
