ID I8V6U0_9BACE Unreviewed; 1162 AA.
AC I8V6U0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=HMPREF1061_01911 {ECO:0000313|EMBL:EIY22180.1};
OS Bacteroides caccae CL03T12C61.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=997873 {ECO:0000313|EMBL:EIY22180.1, ECO:0000313|Proteomes:UP000002965};
RN [1] {ECO:0000313|EMBL:EIY22180.1, ECO:0000313|Proteomes:UP000002965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL03T12C61 {ECO:0000313|EMBL:EIY22180.1,
RC ECO:0000313|Proteomes:UP000002965};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides caccae CL03T12C61.";
RL Submitted (FEB-2012) 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:EIY22180.1}.
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DR EMBL; AGXF01000006; EIY22180.1; -; Genomic_DNA.
DR RefSeq; WP_005675914.1; NZ_JH724079.1.
DR AlphaFoldDB; I8V6U0; -.
DR GeneID; 75114576; -.
DR PATRIC; fig|997873.3.peg.2003; -.
DR HOGENOM; CLU_001493_1_1_10; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000002965; 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; 3.30.720.200; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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..749
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 797..948
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 710..714
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 713
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1162 AA; 132910 MW; 6231A665206E91A2 CRC64;
MGKRFTEYSQ FDLSQVNKDV LKKWDENKVF AKSMTERDGC PSFVFFEGPP SANGMPGIHH
VMARTIKDIF CRYKTMKGYQ VKRKAGWDTH GLPVELSVEK ALGITKEDIG KKISVADYNA
ACRKDVMKYT KEWEDLTHQM GYWVDMKHPY ITYDNRYIET LWWLLKQLYK KGLLYKGYTI
QPYSPAAGTG LSSHELNQPG CYRDVKDTTV VAQFKMKNPK PEMTEWGTPY FIAWTTTPWT
LPSNTALCVG PKIDYVAVQS YNAYTGEPIT VVLAKALLNA LFNPKAADLK LEDYKAGDKL
VPFKVIAEYK GTDLIGMEYE QLIPWVKPVE VSEDGDWKAS NKAFRVIPGD YVTTEDGTGI
VHIAPTFGAD DANVARAAGI PSLFMINKRG ETRPMVDLTG KFYLLNELDE NFVKECVDVE
KYKEYQGAWV KNAYNPVFMI DGKYDEKAAQ AAESLDIVLA MMMKANNQAF KIEKHVHNYP
HCWRTDKPVL YYPLDSWFIR STACKERMME LNKTINWKPE STGTGRFGKW LENLNDWNLS
RSRYWGTPLP IWRTEDGTGE LCIESVEELY NEIEKSVAAG FMKSNPYKDR GFVPGEYTEE
NYDKIDLHRP YVDDIILVSK DGQPMKRESD LIDVWFDSGA MPYAQIHYPF ENKELLDSRQ
VYPADFIAEG VDQTRGWFFT LHAIATMVFD SVSYKAVISN GLVLDKNGNK MSKRLNNAVD
PFTTIEKYGS DPLRWYMITN SSPWDNLKFD VEGVEEVRRK FFGTLYNTYS FFALYANVDG
FEYKEADVPM AERPEIDRWI LSVLNTLIKE VDTCYNEYEP TKAGRLISDF VNDNLSNWYV
RLNRKRFWGG EFTQDKLSAY QTLYTCLETV AKLMAPISPF YADRLYTDLI TATGRDNVVS
VHLAEFPKYQ EEMINKELET RMQMAQDVTS MVLALRRKVN IKVRQPLQCI MVPVLDEEQK
AHIEAVKSLI MNEVNVKEIK FVDGAAGVLV KKVKCDFKKL GPKFGKQMKA VAAAVAEMSQ
EAISELEKNG KYTLNLNGEE AVIEVSDVEI ISEDIPGWLV ANEGKLTVAL EVTVTEELRR
EGIARELVNR IQNIRKSSGF EITDKIKITI SKNTQTDDAV NEYNTYICNQ VLGTSLELVD
EVKDGTELSF DDFSLFVNVI KD
//
