ID A0A024FH05_9FLAO Unreviewed; 1134 AA.
AC A0A024FH05;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=WPG_1588 {ECO:0000313|EMBL:BAO75818.1};
OS Winogradskyella sp. PG-2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=754409 {ECO:0000313|EMBL:BAO75818.1, ECO:0000313|Proteomes:UP000031636};
RN [1] {ECO:0000313|EMBL:BAO75818.1, ECO:0000313|Proteomes:UP000031636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-2 {ECO:0000313|EMBL:BAO75818.1,
RC ECO:0000313|Proteomes:UP000031636};
RX PubMed=24874677; DOI=10.1128/genomeA.00490-14;
RA Kumagai Y., Yoshizawa S., Oshima K., Hattori M., Iwasaki W., Kogure K.;
RT "Complete Genome Sequence of Winogradskyella sp. Strain PG-2, a
RT Proteorhodopsin-Containing Marine Flavobacterium.";
RL Genome Announc. 2:e00490-14(2014).
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}.
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DR EMBL; AP014583; BAO75818.1; -; Genomic_DNA.
DR RefSeq; WP_045471037.1; NZ_AP014583.1.
DR AlphaFoldDB; A0A024FH05; -.
DR STRING; 754409.WPG_1588; -.
DR KEGG; win:WPG_1588; -.
DR HOGENOM; CLU_001493_1_1_10; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000031636; Chromosome.
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; 3.30.720.200; -; 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}; Reference proteome {ECO:0000313|Proteomes:UP000031636};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 22..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 1134 AA; 129560 MW; 9F8B9791F28036E7 CRC64;
MSIKFPEYKG LNLPKVAEEI GNYWEANNIF DKSVSTREGK LPYVFFEGPP SANGLPGVHH
VLARAIKDIF PRYKTMKGFQ VKRKAGWDTH GLPVELGVEK ELGITKEDIG TKITVEEYNE
ACKKAVMRYT DIWNDLTKKM GYWVDMDDPY ITYKSKYMES VWWLLKQIYE KDLIYKGYTI
QPYSPKAGTG LSSHELNQPG TYQDVTDTTV VAQFKANEDS LPDFLQNEGD IYLLAWTTTP
WTLPSNTALT VGSKIDYVLA ETYNQYTFKP MNVVLAKNLV EKQFDGKYNQ VETKPELIDY
KEGDKIIPFY IVKEFKGKDL VGITYEQLLD FNLEFENKQN AFRVISGDFV TTEDGTGIVH
TAPTFGADDA LVAKQAIPEI PPFLVKDEND NLVPLVDLQG KFRKELDEFG GKYVKNEYYN
DGEAPERSID VELAIKLKTE NKAFKVEKYK HSYPNCWRTD KPILYYPLDS WFIKVTDVKG
RMHELNTSIN WKPKSTGEGR FGNWLANAND WNLSRSRFWG IPLPIWRTED GKEQLCIGSV
SELKSEISKS VEAGIMSEDI FADYEVGNMS EANYETIDLH KNVVDKIVLV SPLGKPMNRE
SDLIDVWFDS GSMPYAQWHY PFENKNLIDN NEAFPADFIA EGVDQTRGWF YTLHAIGTMV
FDSVAYKNVV SNGLVLDKNG QKMSKRLGNA TDPFETLSKY GADATRWYMI MNANPWDNLK
FDSDGIAEVS RKFFGTLYNT YSFFTLYTNI DGFNYSEADI ALEERPEIDR WILSELNTLI
QQVDKFYEEY EPTKAARAIS DFTQDYLSNW YVRLSRRRFW KGDYQADKIS AYQTLYTCME
TIAKLGAPIA PFFMDRLYQD LNAVTQKENF ESVHLSEFPQ VNTSAIDKVL ERKMESAQSI
CSLVLSLRAK EKIKVRQPLQ KIMIPVDSQQ QKEEIEAVSD LIKHEVNIKE VELLEDASDI
LVKQIKPNFK VLGPKFGKDM KLISSAVNGF NADDIKKIEQ NGSIGVEING KNITLGLDDV
EITSQDIEGW LVANEGALTV ALDVTINEDL RKEGVARELV NRIQNLRKDS GFEVTDKIDV
QIQNDEQVAA AIASNEDYIK SETLTEDLTI IENLNNGIEI AFDEVNTKLF IQKH
//
