ID M0QNN8_9ACTN Unreviewed; 1075 AA.
AC M0QNN8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
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:GAC70024.1};
GN ORFNames=GS4_30_00960 {ECO:0000313|EMBL:GAC70024.1};
OS Gordonia soli NBRC 108243.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223545 {ECO:0000313|EMBL:GAC70024.1, ECO:0000313|Proteomes:UP000011666};
RN [1] {ECO:0000313|EMBL:GAC70024.1, ECO:0000313|Proteomes:UP000011666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108243 {ECO:0000313|EMBL:GAC70024.1,
RC ECO:0000313|Proteomes:UP000011666};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia soli NBRC 108243.";
RL Submitted (JAN-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:GAC70024.1}.
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DR EMBL; BANX01000030; GAC70024.1; -; Genomic_DNA.
DR RefSeq; WP_007623658.1; NZ_BANX01000030.1.
DR AlphaFoldDB; M0QNN8; -.
DR STRING; 1223545.GS4_30_00960; -.
DR eggNOG; COG0060; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000011666; 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 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:UP000011666};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 45..676
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 724..865
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 75..85
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 642..646
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1075 AA; 119489 MW; BA7BB22D28569383 CRC64;
MTRPEDPAAT ESGSAATTAP VYPIVDLTDG TGRGAPSFPD VERHVLDYWA ADDTFAASIA
NRADAAEFVF YDGPPFANGL PHYGHLLTGY VKDLVPRYQT MRGKRVERRF GWDTHGLPAE
LEAERQLGIT DKSEIESMGV EKFNDYCRTS VLRYTGEWRD YVTRQARWVD FDNDYKTLDI
DFMESVMWAF KALNDKGLIY QGYRVLPYSW YEQTPLSNQE SKLDDAYKMR QDPAVTVRMP
LVVPADSELA ALDGVNALIW TTTPWTLPSN LAIAVNPEIT YAHVRAADGQ QYLLAEARLG
AYAAEIAEPE TLATYQGAQL EGLSYTPPFD FFRGHPNAHR VLLGDYVTTD SGTGVVHLAP
AFGEEDMELA TTYGIEVVQP LDPGGRFTTM VPPYEGLMVF DANPVIIKDL KETGAVLRHE
TIEHSYPHSW RSGKPLIYMA VPSWFVAVSP IKDRMLELNQ EITWAPGHIR DGQFGKWLEG
AKDWNISRNR YWGAPIPVWV SDDPEYPRTD VYGSLDELER DFGVRPTNLH RPYIDDLTRP
NPDDPTGKST MRRVPEVLDC WFESGSMPFA QVHYPFENAD WFDGNAETGE LPHNPGDFIV
EYNGQTRGWF YNLHVLATAL FDRPAVRSVA AHGIVLGDDG QKMSKSKRNY PDVNEVFDRD
GSDAMRWFLM ASPILRGGNL VVTERGIREG VRQALLPLWN AYSFLQLYAE RPATWRTDST
NVLDRYILAK LSATRDAITD SLDVYDVAGA CEAFRGFCEA LTNWYVRRSR ARFWGGQDAD
PEAFDTLYTV LETASRLAAP LLPLATEAVW RGLTGGRSVH LTDWPSADEL PADTALVTAM
DEVQDVCSTA SSVRKANKLR VRLPLPGLTV ASETAEQLRP YTDLIADEMN VKSVTLATEP
EQYGRYELAV NARAAGPRLG KDVQRVIKAV KAGDWSVRTG DDGTEIVTAA DIDLVDGEYT
RRLVAVEPDS TAELPGGRGL VVLDTAVTEE LEAEGWAKDR VRELQDARRS AGLEVSDRIT
VRLVVPAERR DWALRHADLI AGEVLAVGFD VETGPAGAVE LGDGVTADVA KVGTA
//
