ID A0A345HBY5_9FLAO Unreviewed; 1133 AA.
AC A0A345HBY5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 18-JUN-2025, entry version 22.
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=DVK85_07505 {ECO:0000313|EMBL:AXG74095.1};
OS Flavobacterium arcticum.
OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1784713 {ECO:0000313|EMBL:AXG74095.1, ECO:0000313|Proteomes:UP000253951};
RN [1] {ECO:0000313|EMBL:AXG74095.1, ECO:0000313|Proteomes:UP000253951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1502 {ECO:0000313|EMBL:AXG74095.1,
RC ECO:0000313|Proteomes:UP000253951};
RA Li Y., Li D.-D.;
RT "Complete genome sequence of Flavobacterium arcticum type strain SM1502T.";
RL Submitted (JUL-2018) 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=tRNA(Ile) + L-isoleucine + ATP = L-isoleucyl-tRNA(Ile) + AMP +
CC diphosphate; Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, Rhea:RHEA-
CC COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, ChEBI:CHEBI:456215; EC=6.1.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00048359, ECO:0000256|HAMAP-
CC Rule:MF_02003};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|HAMAP-Rule:MF_02003};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_02003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC 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|ARBA:ARBA00007078,
CC ECO:0000256|HAMAP-Rule:MF_02003}.
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DR EMBL; CP031188; AXG74095.1; -; Genomic_DNA.
DR RefSeq; WP_114677853.1; NZ_CP031188.1.
DR AlphaFoldDB; A0A345HBY5; -.
DR KEGG; fat:DVK85_07505; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000253951; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 3.40.50.620:FF:000063; Isoleucine--tRNA ligase; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02003};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02003};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW 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}; Reference proteome {ECO:0000313|Proteomes:UP000253951};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 20..720
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 769..921
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 50..60
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 682..686
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 685
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1133 AA; 128570 MW; D3F9A7E680EDB8CD CRC64;
MSKKFTEYKG LDLPTVAGEV LEFWKKENVF EKSVSTREGK PQYVFYEGPP SANGLPGIHH
VMARAIKDIF CRYQTQKGFQ VKRKAGWDTH GLPVELGTEK ELGITKEDIG TKISVEEYNE
ACKRTVMRYT DVWNDLTEKM GYWVDMEDPY ITYKPKYMET VWWLLKQIYD KGLIYKGYTI
QPYSPKAGTG LSSHEVNQPG AYRDVTDTTI VAQFKTIADT LPEAFKGFGA IDFMAWTTTP
WTLPSNTALT VGPKIDYVLA RTFNQYTFEP INVVLAKSLV GKQFSGKYFE STEDADFENY
TSSDKKIPYQ ILAEAKGKDL VGVKYEQLLP YTLPYQNPEN AFRVIAGDFV TTEDGTGIVH
TAPTFGADDA KVAKEAQPEI PPMLVLDANG TAVPLVDMQG RFIEGMGDLS GKYVKNEYYD
KDEAPEKSVD VEIAIRLKEE NKAFKVEKYV HSYPHSWRTD EPLLYYPLDS WFIKITDVKE
KMFDLNETIN WKPKATGEGR FGNWLKNAND WNLSRSRYWG IPLPIWRTED KTEEMMVGSV
EELYNEIEKA IAAGVMTENP FKGFEAGNMT EENYSLVDLH KNVVDAITLI SPSGKPMQRE
ADLIDVWFDS GSMPYAQWHY PFENKELIDN NTAFPADFIA EGVDQTRGWF YTLHAIATLV
FDKVAYKNVV SNGLVLDKSG QKMSKRLGNA VDPFTTLAEY GPDATRWYMI ANANPWDNLK
FDIEGVAEVR RKFFGTLYNT YSFFALYANI DNFTYAEPEI PIAKRPEIDR WILSELNTLI
KNVDSYYAEY EPTKAARAIS DFVQENLSNW YVRLCRRRFW KGEYAEDKIA AYQTLYTCLV
TVAKLGSAIA PFFMDRLYKD LTQASQSEGF ESVHLAEFPA YADNFVDKSL ESRMEKAQTI
SSLVLSLRKK EMIKVRQPLQ KVMIPVLDAK QKAEIEAVSE LIKAEVNVKE IELLDDASGV
LVKQVKPNFK ALGPRFGKDM GLVSKEIQNF SQEQIAIIDK TGSIDIEISG KSINLTSGDV
EISSQDIEGL LVANANGITV ALDITITEVL KKEGIARELV NRIQNLRKDS GFEVTDKIKV
FLKSDEALQS AVTANEDYIK SETLTEELIF KNEITNGIEI EFDDIKTLVL ISK
//
