ID F5ISW9_9BACT Unreviewed; 1137 AA.
AC F5ISW9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 66.
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=HMPREF9455_00186 {ECO:0000313|EMBL:EGK02064.1};
OS Dysgonomonas gadei ATCC BAA-286.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Dysgonomonas.
OX NCBI_TaxID=742766 {ECO:0000313|EMBL:EGK02064.1, ECO:0000313|Proteomes:UP000004913};
RN [1] {ECO:0000313|EMBL:EGK02064.1, ECO:0000313|Proteomes:UP000004913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-286 {ECO:0000313|EMBL:EGK02064.1,
RC ECO:0000313|Proteomes:UP000004913};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Pudlo N., Martens E.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dysgonomonas gadei ATCC BAA-286.";
RL Submitted (APR-2011) 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:EGK02064.1}.
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DR EMBL; ADLV01000002; EGK02064.1; -; Genomic_DNA.
DR RefSeq; WP_006797688.1; NZ_GL891979.1.
DR AlphaFoldDB; F5ISW9; -.
DR STRING; 742766.HMPREF9455_00186; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_10; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000004913; 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; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000004913};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 20..724
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 772..922
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 685..689
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 688
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1137 AA; 129925 MW; 8B0934FECEE5510A CRC64;
MSKQFSEYNR FNLSDINKEI LEKWDKENIF QQSLDVRTGA PSFVFYEGPP SANGMPGIHH
VMARAVKDIF CRYKTMKGFL VNRKAGWDTH GLPVELSVEK KLGITKEDIG KKISVEEYNN
ACRKEVMKYT GEWENLTRIM GYWVDMNDPY VTYDSRYIET LWYLLNELYK KGYLYKGYTI
QPYSPAAGTG LSTHELNQPG AYRDVKDTTC VAQFKIKSPK AEMSQFGDAY FLAWTTTPWT
LPSNTALAVG ADITYVAVQS YNPYTGNKMT AVLAKWLMFS MFNEKAKDVA LEDYKQGDKL
IPYKVVGEWK GSDLVGMEYE QLIPWMNPGE GAFRVLGGDF VTTDDGTGIV HIAPTFGADD
AKVAKENGVP ALLLLDKDGN QRPMVDLTGK YFRLEDIDPE YLKTNVNVDL YKEYAGRYVK
NEYDDTLPAD ANTLDIDLSV MLKLANQAFK IERQVHNYPH CWRTDKPVLY YPLDSWFICT
TASRERLMEL NETINWKPQS TGTGRFGKWL ENLQDWNLSR SRYWGTPLPI WRTEDGKEEK
CIGSIKELYA EMQKAVNAGF MKEIPWKGFE IGNLDKANYE KIDLHRPYVD NIVLISESGK
PMKREADLID VWFDSGAMPF AQVFYPNISE EEFSKVYPAD FIAEGVDQTR GWFFTLHAIS
TMVKDSISFK NVVSNGLVLD KNGNKMSKSR GNGVDPFSTI EKYGSDPLRW YMITNASPWD
NLKFDIEGVE EVRRKFFGTL YNTYSFFALY ANVDGFTFSE KLIPVSERPE IDRWIISLLN
TLVKDVDEYY ETYEPTKAGR AISDFVNDNL SNWYVRLNRK RFWGGEMTKD KLSAYQTLYT
CLETVAKLMA PISPFYSDKL FYDLVSVTEK EKAPSVHLSD YPAYDASVVD KTLEERMQIA
QDISSAVLAL RRKESVKVRQ PLMQIMIPIL NDKQEQDIEA VRDLILNEVN VKELKYVGGS
EGIFVKKVKP DFKKLGPRYG KIMKQLAVEV QNMPQDAIAA FEKDGSYTFD VEGQAATIEL
ADAEIISEDI PGWLVANAGK LTVALDVTIT EDLRKEGIAR ELVNRIQNIR KSSGFDITDR
INIKISDQEQ IRSTVSEYKT YIASQVLADN IELGNVENGQ EIDMDDYILQ VSVDKVR
//
