ID E4TN29_MARTH Unreviewed; 1120 AA.
AC E4TN29;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 OrderedLocusNames=Ftrac_2465 {ECO:0000313|EMBL:ADR22443.1};
OS Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408
OS / VKM B-1430 / H-43) (Microscilla tractuosa) (Flexibacter tractuosus).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Marivirgaceae; Marivirga.
OX NCBI_TaxID=643867 {ECO:0000313|EMBL:ADR22443.1, ECO:0000313|Proteomes:UP000008720};
RN [1] {ECO:0000313|EMBL:ADR22443.1, ECO:0000313|Proteomes:UP000008720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 /
RC H-43 {ECO:0000313|Proteomes:UP000008720};
RX PubMed=21677852; DOI=10.4056/sigs.1623941;
RA Pagani I., Chertkov O., Lapidus A., Lucas S., Del Rio T.G., Tice H.,
RA Copeland A., Cheng J.F., Nolan M., Saunders E., Pitluck S., Held B.,
RA Goodwin L., Liolios K., Ovchinikova G., Ivanova N., Mavromatis K., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Han C., Tapia R., Ngatchou-Djao O.D., Rohde M., Goker M., Spring S.,
RA Sikorski J., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Marivirga tractuosa type strain (H-43).";
RL Stand. Genomic Sci. 4:154-162(2011).
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}.
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DR EMBL; CP002349; ADR22443.1; -; Genomic_DNA.
DR RefSeq; WP_013454586.1; NC_014759.1.
DR AlphaFoldDB; E4TN29; -.
DR STRING; 643867.Ftrac_2465; -.
DR KEGG; mtt:Ftrac_2465; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_10; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000008720; Chromosome.
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; 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:UP000008720};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 19..702
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 752..905
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 665..669
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 668
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1120 AA; 128886 MW; 784599C4A331D6F1 CRC64;
MGQYKEYKNL NYAELADEVL EFWNKNDIFQ KSMTTREGKP TFTFYEGPPS ANGTPGIHHV
MARAVKDIFC RYKTLKGFQV KRKGGWDTHG LPVELQVEKE LGITKEDIGK KITVAEYNDR
CKKAVMKFKG EWDDLTRKMG YWVDLDDPYI TFDRKYMETL WHLLKKFHDK NLLYKGYTVQ
PYSPAAGTGL SSHELNQPGC YRDVKDTSVT AQFTVKKDDK SAFLFESEEE DVRFIAWTTT
PWTLPSNCAL AVGEKIEYVK VKTFNQYTFE PVSVVLAKDL VSKQFNAKAK DLKLDDYKAG
DKLVPFEIAQ TFKGKDIVET RYEQLMPYVT SEDLEKNAFR VIPGDFVTTE DGTGIVHTAS
VFGADDFKVA QQNNVPAVMV KDEQGKDTPL VDKKGRFVTE VTDFAGKYVK EEYYDDATRN
DPDFKPTDVL IAIKLKEDNK AFKVEKHEHS YPHCWRTDKP ILYYPLDSWF IKTTAMKDRL
VELNKTINWK PASTGEGRFG NWLENLVDWN LSRSRYWGTP LPIWVTEDRK EQICIGSLEE
LRNEVNKSVK AGFMEEELAE DFDLHRPYVD DVILTSESGQ KMFREPDLID VWFDSGAMPY
AQWHYPFENN ETFDKNYPAD FIAEGVDQTR GWFFTLHAIS GMLFDSVAYK NVIANGLVLD
KEGNKMSKRL GNAINPFETI KKYGPDATRW YMIANANPWD NLKFNLQGVE EVQRKFFGTL
QNTYNFFALY ANLDGFTFEG ESIPLEKRTE SDRWILSKLN SLKKAVDVAY DDYEPTRAAR
LIQDFVQDDV SNWYVRLNRK RFWKGEYNED KKAAYQSLYE CLESIAILSA PIAPFYMDNL
FQSLNNISNR MDFESVHLVD FPVADENIIN KDLEERMFLA QHISSLTHSI RKAQKIKVRQ
PLHKILVPVL NDKTRKQIEA VEDLIISEVN VKSIEYIDDA SGVLVKNVKP NFRKLGQHFG
PKMKAVTQII NQWGQEEIAK IEQNDAFEIE VDGEQHTLTL EDVDITSQDI PGWSVASEAG
ITVALDISID DDLRREGFAR DLVNRIQNLR KEKGLEVQDK IAVAVKQGNE LVDTAISQNK
DYICSETQAV SLDLAENLTE TTEIEIDDLR IELSVVVKNL
//
