ID A0A1L3J6Y3_9FLAO Unreviewed; 1133 AA.
AC A0A1L3J6Y3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=LPB144_10965 {ECO:0000313|EMBL:APG60896.1};
OS Christiangramia salexigens.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Christiangramia.
OX NCBI_TaxID=1913577 {ECO:0000313|EMBL:APG60896.1, ECO:0000313|Proteomes:UP000182510};
RN [1] {ECO:0000313|EMBL:APG60896.1, ECO:0000313|Proteomes:UP000182510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0144 {ECO:0000313|EMBL:APG60896.1,
RC ECO:0000313|Proteomes:UP000182510};
RA Kim E., Yi H.;
RT "Gramella sp. LPB0144 isolated from marine environment.";
RL Submitted (NOV-2016) 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}.
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DR EMBL; CP018153; APG60896.1; -; Genomic_DNA.
DR RefSeq; WP_072553585.1; NZ_CP018153.1.
DR AlphaFoldDB; A0A1L3J6Y3; -.
DR STRING; 1913577.LPB144_10965; -.
DR KEGG; grl:LPB144_10965; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000182510; 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; 3.40.50.620; HUPs; 2.
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; 1.
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:UP000182510};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 20..719
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 768..919
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 681..685
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 684
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1133 AA; 129760 MW; 83D08A40180B2F7E CRC64;
MSRRFPEYKG LDLPKVAEEI LNYWDENDIF EKSITTREGK EPFVFFEGPP SANGLPGIHH
VMARAIKDIF CRYKTQKGFQ VKRKAGWDTH GLPVELGVEK ELGITKEDIG TKISIEKYNE
ACKNAVMRYT DVWNDLTQKM GYWVDMEDPY VTYKSKYMET VWWLLSEIYN KDLIYKGYTI
QPYSPKAGTG LSSHELNQPG TYQDVTDTTV TAMFKAKKDS LPDFLKSEDN LFFIAWTTTP
WTLPSNTALT VGPKIEYVTV KTYNQYTFEP ITIVVAKDLA EKQFDKKFKK AESVEELESY
TKEDKKIPYL IGESFTGKDL VGAKYEQLLP YALPNDNPEN AFRVISGDFV TTEDGTGIVH
TSPTFGADDA LVAKQASPEV PPLLVKDENG NLVPLVDLQG KFRPEMGEHA GKYVKNEYYD
EGEAPEKSVD VELAIKLKEE NRAFKVEKYV HSYPNCWRTD KPILYYPLDS WFIKVTEFKD
RMHELNKGIN WKPKSTGEGR FGNWLANAND WNLSRSRYWG IPLPIWRTED GTEVKVIGSV
AQLKEEMQKA VDAGFMKEDI FADFEPGNMS EENYDKVDLH KNVVDGITLV SDSGKPMKRE
ADLIDVWFDS GSMPYSQWHY PFENKEKVEN KWRKADFIAE GVDQTRGWFY TLHAIATMIF
DDVAYKNVVS NGLVLDKNGQ KMSKRLGNAA DPFETISVYG PDATRWYMIS NANPWDNLKF
DIEGIGEVQR KFFGTLYNTY SFFTLYANID KFSYAEDDVA LEDRPEIDRW ILSELHSLIE
KVDKFYADYE PTKATRAISE FVQENLSNWF VRLSRRRFWK GDYEQDKISA YQTLYTCLET
VAKLGAPVAP FYMDRLFRDL NAATGKDKAE SVHTADFPVY EPNFVDKSLE RKMEKAQTIS
SLVLSLRKKE MIKVRQPLQR VMIPVLDEEQ KQEIQAVEDL IKSEVNVKEI QLIDDASGLL
VKQIKPNFRV LGPRFGKDIK LIVSKINQFE ASDIAKIERE GSIEVDINGN LVNLSIDEVE
ISSQDIEGWL VASSGNITVA LDVSISPELK MEGVARELVN RIQNLRKDSG YEVTDTIDVT
LQKDGIIEDA VNENITYIKN ETLTASLEFA EVVKEGVDLE FDEIATKLFI KKH
//
