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Database: UniProt
Entry: A0A0G0VBL4_9BACT
LinkDB: A0A0G0VBL4_9BACT
Original site: A0A0G0VBL4_9BACT 
ID   A0A0G0VBL4_9BACT        Unreviewed;       978 AA.
AC   A0A0G0VBL4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02002};
DE            EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02002};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02002};
DE            Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02002};
GN   Name=ileS {ECO:0000256|HAMAP-Rule:MF_02002};
GN   ORFNames=UU47_C0003G0023 {ECO:0000313|EMBL:KKR97036.1};
OS   candidate division TM6 bacterium GW2011_GWE2_41_16.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=1619075 {ECO:0000313|EMBL:KKR97036.1, ECO:0000313|Proteomes:UP000034748};
RN   [1] {ECO:0000313|EMBL:KKR97036.1, ECO:0000313|Proteomes:UP000034748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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_02002}.
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_02002};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02002};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_02002};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02002}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02002}.
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_02002}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 1 subfamily. {ECO:0000256|ARBA:ARBA00006887,
CC       ECO:0000256|HAMAP-Rule:MF_02002}.
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:KKR97036.1}.
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DR   EMBL; LCAT01000003; KKR97036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0VBL4; -.
DR   STRING; 1619075.UU47_C0003G0023; -.
DR   PATRIC; fig|1619075.3.peg.243; -.
DR   Proteomes; UP000034748; 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; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   Gene3D; 1.10.730.20; -; 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_02002; Ile_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033708; Anticodon_Ile_BEm.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023585; Ile-tRNA-ligase_type1.
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; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 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.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_02002};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02002};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02002};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02002};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02002};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02002};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_02002}; Zinc {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   DOMAIN          28..669
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          721..849
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           57..67
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   MOTIF           638..642
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   BINDING         597
FT                   /ligand="L-isoleucyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:178002"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   BINDING         641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   BINDING         948
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   BINDING         951
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   BINDING         964
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   BINDING         967
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
SQ   SEQUENCE   978 AA;  109741 MW;  25B3985BFA2252D9 CRC64;
     MEYKDTLNLP KTDFPIRPNA KVDDPALIAR WEKESLYTQA MSLNKGSDMF LLHIGPPYAN
     GNIHLGHAYN GILKDIVSKS YRMAGSHVPV RPGWDCHGLP IEIKVTTEQP GLSGVALKTA
     CRAYATKWVD VQRDGFKRLG IVMEWDRPYL TMSPEYESRV VEAFLKLSHA GFIERKLKSV
     AWCASCKTTL ASAEIEYEDR KDPSLYVAMQ FDNGTLTKIF WEKTGLHAQE PVFIVIWTTT
     PWTLPLNRAV SIKEGAFYTV ARCKDRAKIT KTCPDTCPGD AFNNQIGVSQ NSEGYKIIVV
     GSARYDAFNE LLGGICEKIA EIPFDMLKGA QLQHLYDTQR RVPVIIDSEV SLTDGTASVH
     IAPGCGPSDY ELGVKNNLEI YSPLSDEGRY TAGIKPESLE GMSFIDAQIW VIKDLAARGL
     LLFKNSIKHS YPHCWRCHNG LMFRATPQWF FDLKKNAVQD RALAAINDIE FNPKGGQNFL
     RATVETRWEW CLSRQRIWGV PIVALVCEKC GHGLVDKAMG AFIVEHIAKE GIEFWDKVSI
     EELFKHIESS HACSHCSATT WRKESDILDV WFESGLSHYA VLKQDPTLGF PAQLYLEGID
     QHRGWFQSSL LTAIALYGQA PMEGIMTHGF TVDEQGRKMS KSLGNVVNPQ DVVDKIGTDG
     LRLWVASIGN DGDAVMSQKL LDNVTEVYRK IRNTMRFLLQ NLYDYQHERD AVAVKDLMII
     DQYALTRLNV FNERMLKAYS QYDSTALYHG FAEYCTVELS SLYLDVVKDR LYTETAGGVK
     RRSTQTVIWY ILDTLTRLSA PILSCTAELV ADQYQQPGHP SIHLQGFRDV SGECAACRNV
     CALEAVDILV RDMRPLLLRA LEVQRASGAI KHSLEASIHI YLAHDSSFHA PLKDVAAYAR
     DAGSSIEAFI QELLIVSDVV IESAHDDSYS FMGDGVYVRV DHAAGGKCPR CWQWTKSAKE
     DLLCDRCAEI ITSAQRLT
//
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