ID A0A1D9DYL9_9MICO Unreviewed; 1074 AA.
AC A0A1D9DYL9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ECO:0000313|EMBL:AOY55918.1};
GN ORFNames=A4Z71_02750 {ECO:0000313|EMBL:AOY55918.1};
OS Candidatus Rhodoluna planktonica.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Rhodoluna.
OX NCBI_TaxID=535712 {ECO:0000313|EMBL:AOY55918.1, ECO:0000313|Proteomes:UP000243784};
RN [1] {ECO:0000313|EMBL:AOY55918.1, ECO:0000313|Proteomes:UP000243784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-Dar1 {ECO:0000313|EMBL:AOY55918.1,
RC ECO:0000313|Proteomes:UP000243784};
RX PubMed=27659506; DOI=10.1016/j.bbabio.2016.09.006;
RA Nakamura S., Kikukawa T., Tamogami J., Kamiya M., Aizawa T., Hahn M.W.,
RA Ihara K., Kamo N., Demura M.;
RT "Photochemical characterization of actinorhodopsin and its functional
RT existence in the natural host.";
RL Biochim. Biophys. Acta 1857:1900-1908(2016).
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|ARBA:ARBA00007078,
CC ECO:0000256|HAMAP-Rule:MF_02003}.
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DR EMBL; CP015208; AOY55918.1; -; Genomic_DNA.
DR RefSeq; WP_070954430.1; NZ_CP015208.1.
DR AlphaFoldDB; A0A1D9DYL9; -.
DR STRING; 535712.A4Z71_02750; -.
DR KEGG; rpla:A4Z71_02750; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000243784; 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; IPR001412; aa-tRNA-synth_I_CS.
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.
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_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|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:UP000243784};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 28..669
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 720..857
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 61..71
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 635..639
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 638
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1074 AA; 120357 MW; E15B2FB90F670009 CRC64;
MYPKNKKASN DARDGVNPSP SFPKIEEQIL EFWQQDSTFQ ASIDQRAAEN AQEFVFYDGP
PFANGLPHYG HLLTGYAKDM IPRFKTMQGY RVERRFGWDT HGLPAEVEAE RQLGISGRPE
IEKYGIDKFN EYCKTSVLKY TEDWRTFVTR QARWVDFDND YKTLDASFTE SVIWAFSELH
KKGLVYEGFK VLAYCWRCET PLSNHELRMD DEVYRQRQDQ TLTVTFPISD GQKFAQAKLL
AWTTTPWTLP TNFALAVGSK IRYVLIPAGE AGSADGLGGK FILAKTQVGA YAKDLGYADA
EAALAAIEEE FDGSELAGIR YERLFDYYAD SEKFDVANAW QVLVDDYVTD GDGTGIVHQA
PAYGEDDQRV CNAAGIPTYV SVDERACFNS LVTDFVGQHV FEANKPISQL LKANSRVLRQ
ASFEHPYPHC YRCKNPLIYK AVSSWFVETT KLRERMLELN QEINWTPEHT KDGSFGKWLE
NVRDWAISRN RFWGAPIPVW KSDDPNYPRI DVYGSLDEIE RDFGVRPTDF HRPYIDELVR
PNPDDPTGKS MMRRVPEVLD CWFESGSMPY AQVHYPFENT DWFETHNPGD FIVEYVGQTR
GWFYTLHVLS TALFDRPAFK SAISHGIILG NDGQKMSKSL RNYPDVNEVF DRDGADAMRW
FLLSSPILRG GNLIVTEQGI REGVRQVLLP LWNTWYFFSL YANAAKYEAK TSFSSQDVLD
RYLLAKTSDL ITEVEGHFNR YDSYSAAASL RDFADLLTNW YVRRSRDRFW DGSPEAFDTL
YTVLEAVCRV SAPLLPMVTE EIWQGLTGGR SVHLESWPNA ENFPADAALV EAMDKVRAIS
SSAQALRKGA GLRVRLPLAK LTVVTKNANL LSDFSSILTD ELNVKAVDLV ELSLDSTSEF
GVTKRLTVNS RAAGPRIGKD VQAVIAAAKS GNWVEDSGSV VAGGIALIEG EYEINLVADT
DAEQNATNHI GILTGGGFLI LDGKLTPELE AEGLARDVIR AVQQARKDAD LDVSDRIALS
LTGSAEVIAA VGAHQALVMA ETLTLQLETK EEPVSAGATV GNDLFVAIKV AKLG
//
