ID B0NPH8_BACSE Unreviewed; 1162 AA.
AC B0NPH8;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 82.
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:EDS15942.1};
GN ORFNames=BACSTE_01388 {ECO:0000313|EMBL:EDS15942.1};
OS Bacteroides stercoris ATCC 43183.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=449673 {ECO:0000313|EMBL:EDS15942.1, ECO:0000313|Proteomes:UP000004713};
RN [1] {ECO:0000313|EMBL:EDS15942.1, ECO:0000313|Proteomes:UP000004713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43183 {ECO:0000313|EMBL:EDS15942.1,
RC ECO:0000313|Proteomes:UP000004713};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides stercoris(ATCC 43183).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS15942.1, ECO:0000313|Proteomes:UP000004713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43183 {ECO:0000313|EMBL:EDS15942.1,
RC ECO:0000313|Proteomes:UP000004713};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) 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:EDS15942.1}.
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DR EMBL; ABFZ02000018; EDS15942.1; -; Genomic_DNA.
DR RefSeq; WP_005654116.1; NZ_DS499672.1.
DR AlphaFoldDB; B0NPH8; -.
DR GeneID; 31796810; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_10; -.
DR Proteomes; UP000004713; 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; 132473 MW; ADFDB08280DA6C2D CRC64;
MGKKFAEYSK FDLSEINKEV LKKWDENQVF AKSMTEREGC PSFVFFEGPP SANGMPGIHH
VMARSIKDIF CRYKTMKGFQ VKRKAGWDTH GLPVELGVEK ALGITKEDIG KTISVAEYNA
ACRKDVMKFT KEWEDLTHKM GYWVDMQNPY ITYDNRYIET LWWLLKQLHK KGLLYKGYTI
QPYSPAAGTG LSSHELNQPG CYRDVKDTTV VGQFKMKNPK PEMAEWGTPY FLAWTTTPWT
LPSNTALCVG PKIDYVAVQT YNGYTGEKMT VVLAKALLYT HFNKKAEELA LEDYKPGDKL
IPFKIVGEYK GPDLAGMEYE QLIPWVKPVE VDNDGNWSVS DKGFRVILGD YVTTEDGTGI
VHIAPTFGAD DAFVARAAGI PSLFMINKRG ETRPMVDLTG KFYLLDELDE RFVKECVDVD
AYKEYQGRWV KNAYDPQFTV NGKYDEKAAQ AAETLDIYIC MMMKAANQAF KIEKHVHNYP
HCWRTDKPVL YYPLDSWFIR STACKERMIE LNKTINWKPE STGTGRFGKW LENLNDWNLS
RSRYWGTPLP IWRTEDGDEE KCIESVEELY NEIEKSVAAG LMSSNPYKDK GFQPGVYTQE
NYDKIDLHRP YVDDIVLVSK AGKPMKRESD LIDVWFDSGS MPYAQIHYPF ENKELLDSHQ
VYPADFIAEG VDQTRGWFFT LHAIATMVFD SISYKAVISN GLVLDKNGNK MSKRLGNAVD
PFSTIEKYGS DPLRWYMITN SSPWDNLKFD VDGVEEVRRK FFGTLYNTYS FFALYANVDG
FEYKEADVPM AERPEIDRWI ISVLNTLVKD VDNCYNEYEP TKAGRLISDF VNDNLSNWYV
RLNRKRFWGG GMTQDKLSAF QTLYTCLETV AKLMAPIAPF YADMLYSDLT AATGRDNVVS
VHLAKFPECK EEMIDKELEA RMQMAQDVTS MVLALRRKVN IKVRQPLQCI MVPVVDEEQR
AHIEAVKALI MNEVNVKEIK FVDGAAGVLV KKVKCDFKKL GPKFGKQMKA VAAAVAGMPQ
EAIAELEKNG SYTLNLDGAE AVIETSDVEI FSEDIPGWLV ANEGKLTVAL EVTITEELRR
EGIARELVNR IQNIRKSSGF EITDKIKITL SKNPQTDDAV NEYKDYICNQ VLGTSLTLTD
NVEGGTELEF DDFRLYVSVV KE
//
