ID D1PV24_9BACT Unreviewed; 1235 AA.
AC D1PV24;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 69.
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:EFA44744.1};
GN ORFNames=HMPREF0645_0809 {ECO:0000313|EMBL:EFA44744.1};
OS Hallella bergensis DSM 17361.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hallella.
OX NCBI_TaxID=585502 {ECO:0000313|EMBL:EFA44744.1, ECO:0000313|Proteomes:UP000003160};
RN [1] {ECO:0000313|EMBL:EFA44744.1, ECO:0000313|Proteomes:UP000003160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17361 {ECO:0000313|EMBL:EFA44744.1,
RC ECO:0000313|Proteomes:UP000003160};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (OCT-2009) 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:EFA44744.1}.
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DR EMBL; ACKS01000034; EFA44744.1; -; Genomic_DNA.
DR AlphaFoldDB; D1PV24; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_10; -.
DR Proteomes; UP000003160; 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 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; 2.
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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000003160};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 39..702
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 725..825
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 878..1024
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 69..79
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 786..790
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 789
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1235 AA; 141821 MW; 85D81305A65B15B2 CRC64;
MFIVGGESLF PLEGKERYTM AKKFAEHTGL DLTKTNEEIL KEWEKNDIFH KSIDEREGCP
QFIFFEGPPS ANGHPGIHHV LARAIKDAFN RYKTMQGFKV ERKAGWDTHG LPVELSVEKE
LGITKKDIDN KASDKYISVE EYNHRCRENV MKFTAEWRNL TEKMGYFVDL DHPYITFDNK
YIETLWWLLK QLYNKGMLYK GYTIQPYSPA AGTGLSSHEL NQPGCYRDVK DTTVTAQFLI
KDAKAEWCKH GEPWFLAWTT TPWTLPSNVA LCVGPKIDYV AVETYNPYNG APMTAIMAES
RVSAYLNADQ ECKDGELLPF DKEKKQCPWR IIEHMKGTEL EGLRYEQLMP WVKPCEKIGD
FAPDFVNEYA GKHPEKVFAS NEGIDQFVEM HEEAFRIILG DYVTTEDGTG IVHIAPTFGA
DDAKVAKDAK VPALYLISKK GETRPMVDLQ GKYYTLDELD KNFVERCVDT KAYEHHAGDY
VKNAYSPEFN TNGVWDAKAS EKAEDLNIIM SMEMKQEGSA FKIEKHVHNY PHCWRTDKPV
LYYPLDSWFI RDTAMKERMV ELNKTIRWQP ESTGTGRFGN WLENLNDWNL SRSRFWGTPL
PVWRDENHNE KCIGSVEELY NEIEKSVAAG VMKNNPLKDK GFVPGDYSQE NYDRIDLHRP
YIDYVVLVND EGKPMYRESD LIDVWFDSGA MPYAQLHYPF EGAINAEGLK KTGMSEAEYR
ASLVNSTYEG TPVAPAFFPA DFINEGVDQT RGWFFTLHAI ATMVFDSVSF KNVISSGLVL
DAKGNKMSKH VGNVTNPFEM IEKYGADPVR FYMMTNSEPW DNLKFDPNGI DEVRRKFFGT
LYNTYSFFAL YANVDNYDPE QYLKMLQGDS REDLKEIDRW ILSCLNTLVK NVTHELEDYD
PTRAGRLIDS FVNNDLSNWY VRLNRKRFWG KEMSEDKIAA YNTLYTCLMT VSKLLAPFAP
FYADELYHDL GGKLLSVHLD QFPVADDNWI DTDLEMRMSM AQKITSMVLA LRRKVNIKVR
QPLQQIMIPA IDEDQRSHIE AMKDLIVTEV NVKELQFAEG QSVLVKKVKC NFRVMGKKFG
KHMKAVASRM NALSQEEIAQ LERQGNYSFE VDGQNLTVEA ADVEIISEDI PGWLVSNEGN
LTVALEVELT DALRQEGMAR ELINRIQNLR KETGLEITDR IQVTIAPHEQ TDAAIHAFED
YIKSQVLADE LTIADNDGEK TAFDDFELNI KVVKK
//
