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Entry: A0A1F5SD75_9BACT
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ID   A0A1F5SD75_9BACT        Unreviewed;      1033 AA.
AC   A0A1F5SD75;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=A3H66_02320 {ECO:0000313|EMBL:OGF24670.1};
OS   Candidatus Falkowbacteria bacterium RIFCSPLOWO2_02_FULL_45_21.
OC   Bacteria; Candidatus Falkowbacteria.
OX   NCBI_TaxID=1797989 {ECO:0000313|EMBL:OGF24670.1, ECO:0000313|Proteomes:UP000178783};
RN   [1] {ECO:0000313|EMBL:OGF24670.1, ECO:0000313|Proteomes:UP000178783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGF24670.1}.
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DR   EMBL; MFFW01000003; OGF24670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5SD75; -.
DR   STRING; 1797989.A3H66_02320; -.
DR   Proteomes; UP000178783; 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   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}; Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT   DOMAIN          59..681
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          754..903
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          34..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           71..81
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT   MOTIF           648..652
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT   BINDING         651
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1033 AA;  118259 MW;  E2C5CC020DF73DB6 CRC64;
     MIDKKSDSKQ STNPFPKMEE QVLDFWEKNK IFEKSVNNPP GEPRPNPLLR KERGSYQGGK
     KRDYVFYDGP PFITGLPHYA TLLPSIAKDV VPRFWAMKGY RVERVWGWDC HGLPAENQVE
     KQLGLRNKKD IEKLGVDKFI DACRIYVDQG SEQWQWYINR IGRWVDMKHA YRTMDLNYME
     SVIWAFKELY HQGLIYEGYR SSLHCPRCAT PLSKFEITMD AGSYRDVTDN TVVVKFKLKG
     KTPSTPLLKG GKNVYLLAWT TTPWTLPGNL ALAVGEKIKY AEVESAGEYY IIAEEKVKDI
     FKDKKHEIIK KFAGKDLINL NYEPIFDLNN KQIAEDKNVF KIYGGEFVST EEGTGVVHIA
     PNFGEDDFEL GKKQSLPVVD LMDENGIYTK NAGAWFGHYF SKAGAKVLAD LGDKLFSSFA
     YAHSYPFCYR CGTPLIYRAQ KAWYLKISAI REKLLKNGEK VNWIPEHFKS GRFRYNLKSA
     PDWSLSRSRY WGSPIPVWKC SGLAEVKSQK SKVKSGYKNN QPCDNIKVVG SIKELEGLSG
     KKIIDLHKPA IDEVEFTCTQ CGGTMKRVRE VLDCWFESGA MPFAQFHYPF NRQDEWQRLF
     PADFIIEYTG QLRGWFYYLH VLANSLFNNV AFKNVIVTGV LAGTDGRKMS KSYGNYPDPK
     ATLEKYTSDA IRMYFMSSPI MVGDDMSLSE IDIQNTLRKN IILLWNVFKF YELYAISPNP
     LLIKEGEVLT LTKREISARG GSASGGKEGV NILDQWILAR LNQLIGEVTE SMDKYDLPRA
     ARPITDFIND ISTWYLRRSR ERYKSEDVAD KNNALTVTKH VLIELAKIMA PFMPFMAETI
     WQKVTELDFK DKNRSVHLEA WPKTQITDKG GERVLTEMAK VRKVVELGLA KRDEAGIKVR
     QMLSELRIIN YELGKDYEGL LKDELNVKKV TVKNGKGEIK AELDTTITED LRLDGLKREI
     VRLVNNMRKN AGLTIKDKII LSWHSDSEMV KKVFKETAGE LKKDTLSEKI TENEAGGEAV
     KVNGEKVRLG IKI
//
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