ID A0A3A9GP17_9FIRM Unreviewed; 1051 AA.
AC A0A3A9GP17;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=D7Y06_08570 {ECO:0000313|EMBL:RKJ65871.1};
OS Roseburia sp. 1XD42-69.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=2320088 {ECO:0000313|EMBL:RKJ65871.1, ECO:0000313|Proteomes:UP000279120};
RN [1] {ECO:0000313|EMBL:RKJ65871.1, ECO:0000313|Proteomes:UP000279120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1XD42-69 {ECO:0000313|EMBL:RKJ65871.1,
RC ECO:0000313|Proteomes:UP000279120};
RA Liu C.;
RT "Murine metabolic-syndrome-specific gut microbial biobank.";
RL Submitted (SEP-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|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:RKJ65871.1}.
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DR EMBL; RAZG01000013; RKJ65871.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9GP17; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000279120; 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:UP000279120};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 20..632
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 689..838
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 602..606
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 605
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1051 AA; 121104 MW; 31DC7A32C55A796D CRC64;
MYNKVETNLN FVEREKATEQ FWKDNDIFKK SMENRREGET YTFYDGPPTA NGKPHIGHVL
TRVIKDMIPR YQTMKGKYVP RKAGWDTHGL PVELEVEKLL GLNGKEQIEA YGMEPFIKKC
KESVWKYKGM WEDFSGTVGF WADMDEPYVT YDDNFIESEW WALKQIWDKK LLYKGFKIVP
YCPRCGTPLS SQEVAQGYKT VKERSAVVRF KVIGEDAWFL AWTTTPWTLP SNVALCVNPE
ETYCKVKAND GYVYYMAQAL LDKVLGKLAE EGESAYEVLE TYKGTDLERK EYEPLFDFAS
GIIEKQRKKA HYITCDSYVT MTDGTGIVHI APAFGEDDAQ VGRKYDLPFV QLVNGKGELT
EETDYAGVFV KKADPVILTD LEKKGLLFDA PKFEHDYPHC WRCDTPLIYY ARESWFIKMT
EVKEDLIRNN NTVNWIPESI GKGRFGDWLE NIQDWGISRN RYWGTPLNVW ECECGHQECI
GGREELAKRT GNKEDEKVEL HRPYIDEVTF DCPDCGKEMR RVPEVIDCWF DSGAMPFAQH
HYPFENKDLF EQQFPAKFIS EAVDQTRGWF YSLMAESTLL FNKSPYENVI VLGHVQDENG
QKMSKSKGNA VDPFEALKTY GADAIRWYFY INSAPWLPNR FHGKAVQEGQ RKFMGTLWNT
YAFFVLYANI DNFDAAKYAL EYEKLSVMDK WLLSKLNTLI KDVDTNLGNY RIPEAARALD
GFVDEMSNWY VRRSRERFWA KGMEQDKINA YMTLYTALVT VSKCAAPMIP FMTEDIYQNL
VRKVDASAPE SVHLCDFPSA DESVIDKELE KDMDLVLKVV VLGRACRNQA NIKNRQPIGR
MFIKAPFELS EFYTEIIADE LNVKKVEFSQ DVSAYTSYSF KPQLRTVGPK YGKYLSQIKK
ALEELDGNQA MAELNSKGAI KLDSVSEEVV LLNEDLLITM TQMEGYVAEN DNDITVVLDT
NLSEELIEEG FVRELISKIQ TMRKEAGFEV MDRIAVGYQS GEKVSGIFEK NRDIIQAEVL
ADVITTENLS GYMKDWNING EKVTLEVKKQ S
//
