ID A0A0R2TEV1_9FLAO Unreviewed; 1120 AA.
AC A0A0R2TEV1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=ABR87_05260 {ECO:0000313|EMBL:KRO83883.1};
OS Cryomorphaceae bacterium BACL7 MAG-121220-bin83.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655595 {ECO:0000313|EMBL:KRO83883.1, ECO:0000313|Proteomes:UP000051535};
RN [1] {ECO:0000313|EMBL:KRO83883.1, ECO:0000313|Proteomes:UP000051535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL29 MAG-121220-bin83 {ECO:0000313|EMBL:KRO83883.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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:KRO83883.1}.
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DR EMBL; LICF01000003; KRO83883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2TEV1; -.
DR Proteomes; UP000051535; 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; 3.40.50.620; 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..709
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 758..904
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 671..675
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 674
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1120 AA; 125691 MW; 769E775CF28712EA CRC64;
MSHLFPERGS LNLPQTQRDI LQYWEDHDVF AKSIHAQGPA FVFYEGPPSA NGLPGIHHVM
ARALKDVFCR YKTQKGFKVD RRAGWDTHGL PVELGVEKEL GITKEDIGKK LSVAEYNAAC
QEAVMRYTDV WNNLTRQMGY WVDMENPYVT YTSKYMETVW WLLAQINQKG FLYKGYSIQP
YSPKAGTGLS SHELNQPGCY RDVMDVSATA LFAIQASPQA TNLFGDEPVH FMAWTTTPWT
LPSNTALTVG PKIPYTLVDT FNPYTHEKQR VVLAEALISK HFRDEDQGAE GKPEGKILPW
KVRKTFRGKD LLGLRYAQLL PYALPYEHAE NAFQVIPGDF VTTEDGTGIV HTAPTFGADD
ARVAAAAGIP PLLVLDAQGT PVPLVDLQGR FVPQMGDLAG QYVKIEYYAE EEKPERSVDE
QIAIRLKQEG KAFRVQKYAH SYPHCWRTDK PVLYYPLDSW FIKTTAVKER LQALNQEIQW
KPASTGTGRF GNWLENLNDW NLSRSRYWGI PLPIWRTEDG SETVVIDSIE TLRNALEKSV
AAGHMTQNPL EGFVPGDYSE DNYAQVDLHR PHVDQWILTS STGAPMMRET DLIDVWFDSG
SMPYAQVHYP FENKEAIDQN KAFPADFIAE GVDQTRGWFF TLHAIAGLVF DSVAYKAVIS
NGLVLDKNGQ KMSKRLGNAV DPFKAMDTYG SDALRWYMLT NAQPWDNLKF DFAGVQEVQR
KFFGTLHNTY SFLALYAQVD GFDPKQPQVP LAERPEIDRW ILSKLNTLIL DVTAALDDFE
PTRGFRPISD FVQDELSNWY VRLCRRRFWK GQMGPDKLAA YQTLYTCLDT VARLIAPVAP
FYADQLYRDL HPEALSVHTS VFPIVNQGQI DADLERRMDL AQRLSSLVLS VRKKEKIRVR
QPIARVLVPV LNEVQYADVG AIEDLVLAEV NAKALERVDA SSGVFVKRAK ANFKTLGPKA
GSKMKEVAAA IAGLGPDAID TLEQHNTFEL SLPSGAFTLA LEDVEVQTDD IPGMAVASER
GTTLAVDLVL TPALLQEGLA REVVNRIQGL RKDSGLEITD RIQVWVSGAT ETLAAIAAYT
EYIKAEVLAD RLSTDVPPSH IFTLETELEG HLATFAMQRA
//
