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Database: UniProt
Entry: D0GMB5_9FUSO
LinkDB: D0GMB5_9FUSO
Original site: D0GMB5_9FUSO 
ID   D0GMB5_9FUSO            Unreviewed;       932 AA.
AC   D0GMB5;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 87.
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   ECO:0000313|EMBL:EEY34716.1};
GN   ORFNames=HMPREF0554_1329 {ECO:0000313|EMBL:EEY34716.1};
OS   Pseudoleptotrichia goodfellowii F0264.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Pseudoleptotrichia.
OX   NCBI_TaxID=596323 {ECO:0000313|EMBL:EEY34716.1, ECO:0000313|Proteomes:UP000004226};
RN   [1] {ECO:0000313|EMBL:EEY34716.1, ECO:0000313|Proteomes:UP000004226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0264 {ECO:0000313|EMBL:EEY34716.1,
RC   ECO:0000313|Proteomes:UP000004226};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (OCT-2009) 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_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:EEY34716.1}.
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DR   EMBL; ADAD01000134; EEY34716.1; -; Genomic_DNA.
DR   RefSeq; WP_006807618.1; NZ_ADAD01000134.1.
DR   AlphaFoldDB; D0GMB5; -.
DR   eggNOG; COG0060; Bacteria.
DR   Proteomes; UP000004226; 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   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 1.10.730.20; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 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   InterPro; IPR010663; Znf_FPG/IleRS.
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   Pfam; PF06827; zf-FPG_IleRS; 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}; Reference proteome {ECO:0000313|Proteomes:UP000004226};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   DOMAIN          38..644
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          688..844
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          896..925
FT                   /note="Zinc finger FPG/IleRS-type"
FT                   /evidence="ECO:0000259|Pfam:PF06827"
FT   MOTIF           64..74
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   MOTIF           605..609
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   BINDING         564
FT                   /ligand="L-isoleucyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:178002"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   BINDING         608
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   BINDING         899
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   BINDING         902
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   BINDING         919
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT   BINDING         922
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
SQ   SEQUENCE   932 AA;  107912 MW;  7B57D9A123254E43 CRC64;
     MSEEKNVEKP DYAGTLNLPK TSFKMKANLA QKEPLTLRDW KKTNIYEKSL KDEGQYFVLH
     DGPPYANGDI HIGHALNKVL KDIILKYKRL RGYNAPYIPG WDTHGLPIEW KIMEEYGEKA
     RNMTPLQIRQ ECKKYALKWV EKQKAEFIRL GILGNWDDPY ITLKPEYEAE QLKVFKEIYE
     NGYVYKGLKP VYWSPTTETA LAEAEIEYKD VVSPSIYVKM EASKDLLDKL GTDEASIVIW
     TTTPWTLPAN LGIALNKDFD YGLYKTEKGN LVLAKELAEK AFGEMKLSYE LIKEFKGNKL
     ERTHYKHPFL DREGLVILGE HVTLDAGTGA VHTAPGHGVD DYVVGQAYGI GILSPVDDQG
     HMTKEAGKYE GLFYKKASKV IVEDIEASGH LMAYSEFTHS YPHDWRSKKP VIYRATEQWF
     ISVDESDVRQ NALKALEDVE FVPEWGKNRI NAMLETRPDW TISRQRVWGV PIPLFYNAET
     NEVIYEPEIM DKVIEAVKKK GTDIWWKYEA EEIIGEELLE KYNLKGVKLR KERSIMDVWF
     DSGASHRGVL IPRGLHRPAD LYLEGSDQHR GWFQSSLLTS IASTKDAPYK RILTHGFVMD
     GQGRKMSKSL GNTIVPKDII EKYGADILRL WVSSVDYRED VRISENILQQ MSDAYRRIRN
     TARFLMGNLN DFDYENKKVD YEEMYEIDKW ALHKLEELKE KTTEYYDKYE FYSLFQEITY
     FCSIDMSAFY LDIVKDRLYC EEKDSIERRS AQTVLTEVLK VLVRVISPVL SFTAEEIWER
     IPESLKKEES VHLSEWVELE PKYKNNELAK KWDKIQNLRK EVNKKLEAAR QEGLIGHSLD
     ARVLLNVNND DYSFLKDYTE DEVSDLFIVS QTKFVNDELG ASEISGISIG VIKALGKKCE
     RCWKYHEEVG NDPEHPDVCP RCAKVLKFAG NK
//
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