ID A0A2M9C301_9FLAO Unreviewed; 1151 AA.
AC A0A2M9C301;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=CLV73_3193 {ECO:0000313|EMBL:PJJ64824.1};
OS Chryseobacterium geocarposphaerae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1416776 {ECO:0000313|EMBL:PJJ64824.1, ECO:0000313|Proteomes:UP000228740};
RN [1] {ECO:0000313|EMBL:PJJ64824.1, ECO:0000313|Proteomes:UP000228740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27617 {ECO:0000313|EMBL:PJJ64824.1,
RC ECO:0000313|Proteomes:UP000228740};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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:PJJ64824.1}.
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DR EMBL; PGFD01000002; PJJ64824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9C301; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000228740; 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; 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 {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 19..742
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 788..941
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 703..707
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 706
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1151 AA; 131623 MW; 6B5E3FAE56F144C4 CRC64;
MSQFKEYKNL NLIDVAENVA EFWKQNKTFN KSVEIREGQP EFVFYEGPPS ANGMPGIHHV
MARALKDIFC RYQTQNGKQV FRKAGWDTHG LPVELGVEKE LGITKEDIGK KISIEDYNKA
CREAVMRYTD VWNNLTEKIG YWVDLEDPYI TYKSKYMETV WWLLKQLYDK GLLYKGYTIQ
PYSPKAGTGL SSHEVNQPGA YRDVSDTTVV AQFKTLPETL PSFLQGFGDV HFLAWTTTPW
TLPSNTALTV GPKIDYVLIK TFNQYTFEPV NVVLAKALVG KQFAKKYAEG TEEDFANYTS
ESKVIPYQIL AEFKGADLVG IKYEQLLDYA KPHQNPENAF RVISGNFVTT EDGTGIVHTA
PTFGADDAKV AKEATPEVPP MLVLDENGNP VPLVDLQGRF LSVVSDEIYG FANEYVKGEY
LSEEEKNIEF NIQKDKLKAI ISDLKAYLSV DERIALKLRK ENKAFKVEKY VHSYPHSWRT
DEPLLYYPLD SWFVKMTAVK DSLVNLNKEI NWKPKATGEG RFANWLENVN DWNLSRSRYW
GIPLPIWRTD DLKEEKIIGS VEELYNEIEK SIAAGFMKEN PFKGFIIGNM SEQNYALVDL
HKNVVDKVIL VSDSGRAMKR ESDLIDVWFD SGAMPYAQLH YPFENKELID NNKAFPADFI
AEGVDQTRGW FYTLHAIGTA VFDSVAYKNV MSNGLVLDKE GQKMSKRLGN AVDPFETLSI
YGPDATRWYM ISNANPWENL KFDIAGIDEI RRKFFGTLYN TYSFFALYAN VDGFNYSEKE
VQNRPEIDRW ILSELNLLIK EVKSFYEDYE PTKVARAINT FVNDNLSNWY VRLCRRRFWK
GDYSEDKISA YQTLYTCLEV VAKLSAPIAP FFMDQLYQDL NKVTGKETAE SIHLTDFPVP
DESLIDADLV EKTHLAQNIT SMVFSLRKKE NVKVRQPLQK VLIPVLDSKT EEQISAVSEL
IKQEVNVKEI QLINTEEAAH LIVKQIKPNF KALGPKLGKD MKTVGGEIAN LDAEHISKLE
KEGKLDIQGY EITLDDVEIS TKDIPGWTVT SDGKTTVALD LTLTDELKSE GIAREFINRV
QNLRKDKDFD LTDRIHISLE ENSPFLEDIK KNEEYISAEV LSNKIEIVSS LSNFNEIEID
EVNFKVNVEK I
//
