ID SYI_HALMA Reviewed; 1074 AA.
AC Q5UZ84;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02003};
DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02003};
DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02003};
GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02003}; OrderedLocusNames=rrnAC2634;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02003};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02003};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_02003}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02003}.
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DR EMBL; AY596297; AAV47419.1; -; Genomic_DNA.
DR RefSeq; WP_011224343.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5UZ84; -.
DR SMR; Q5UZ84; -.
DR STRING; 272569.rrnAC2634; -.
DR PaxDb; 272569-rrnAC2634; -.
DR EnsemblBacteria; AAV47419; AAV47419; rrnAC2634.
DR GeneID; 40153513; -.
DR KEGG; hma:rrnAC2634; -.
DR PATRIC; fig|272569.17.peg.3231; -.
DR eggNOG; arCOG00807; Archaea.
DR HOGENOM; CLU_001493_1_1_2; -.
DR Proteomes; UP000001169; Chromosome I.
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 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; 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; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..1074
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098576"
FT MOTIF 50..60
FT /note="'HIGH' region"
FT MOTIF 605..609
FT /note="'KMSKS' region"
FT BINDING 608
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1074 AA; 122156 MW; D476C7E610567942 CRC64;
MERFAAVDDQ YDPDAVEDGV FEYWDDVDAY EQTKAHRADG EDYFFVDGPP YTSGAAHMGT
TWNKTLKDCY IRYLRMQGYN VTDRPGYDMH GLPIETKVEE RLDFENKKDI EQFGEENFIE
ECKDFAEEQL EGLQTDFQDF GVWMDWDDPY KTVNPEYMEA AWWGFQQAHE RDLVEQGQRS
INQCPRCETG IANNEVEYHD VGKPSIYVKF PLAEQDGSLV IWTTTPWTIV ANTFVAADGD
LEYVGVDAEK DGDTERLYLA EACVEDVLKA GRYDDYEVVE ELSGEEMVGW AYEHPLAEEV
PDHAQGEGSG QVYTADYVEA DRTGLVHSAP GHGEEDFERG QELDLEIFCP VGSDGVYTDD
AGKYAGTFVR DANDEVIDDL DENGVLLSSE PGHTVREGQC WRCDTDIVRI VTDQWFITVT
DIKDELLANI EDSEWYPQWA RDNRFRDFVE DAPDWNVSRQ RYWGIPIPIW LPEDWSGDMD
DAIVVGDREE LAERVDQDID PENVDLHKGT VDDLTITEDS TTYTRVGDVF DVWLDSSVAT
WGTVNYPEQT EDFEELWPAD LIMEAHDQTR GWFWSQLGMS TAATGEIPYK QVLMHGYANM
PDGRGMSKSK GVLIDPHEVI EKHGRDPMRL FLLSVTAQGE DMNFSWEETA EMQRRLNILW
NVARFPLPYM RADDFDPEET TVEDLRDDLE LVDEWVLSRL QSVTEAMTDS MDDFENDKAV
DELLEFVVED VSRFYIQVVR ERMWEEEDSA SKQAAYATLY RVLESVAALF APFTPFVAEQ
VYGALTGDAG HPTVHMCDWP EVDADLHDPA LEREIEVVRE VEEAGSNARQ QAERKLRWPV
TRVVVDVDSD DVADAVRAQE AIIADRLNAR AVEVVGADDE WGELQYSAEA DMSELGPAFG
DDAGRVMNAL NEARVTEQSL DTLEGTVREA LGEDVDLTEE MVEFRRETPE GVTGTEFTAL
DGGGVVYVDT ALTEDIESEG YAREVIRRIQ EMRKDLELDI EERIAVDLTI DDERVDSLVR
EHEALIKEEV RADELDGVED GHRKTWEVEG TDMEIAIAPC EADQREASEQ ASGD
//
