ID D5UD16_CELFN Unreviewed; 1072 AA.
AC D5UD16;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 82.
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 OrderedLocusNames=Cfla_1455 {ECO:0000313|EMBL:ADG74353.1};
OS Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM
OS 18109 / NBRC 3775 / NCIMB 8073 / NRS 134).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG74353.1, ECO:0000313|Proteomes:UP000000849};
RN [1] {ECO:0000313|EMBL:ADG74353.1, ECO:0000313|Proteomes:UP000000849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 /
RC NCIMB 8073 / NRS 134 {ECO:0000313|Proteomes:UP000000849};
RX PubMed=21304688; DOI=10.4056/sigs.1012662;
RA Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Cellulomonas flavigena type strain (134).";
RL Stand. Genomic Sci. 3:15-25(2010).
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; CP001964; ADG74353.1; -; Genomic_DNA.
DR RefSeq; WP_013116687.1; NC_014151.1.
DR AlphaFoldDB; D5UD16; -.
DR STRING; 446466.Cfla_1455; -.
DR KEGG; cfl:Cfla_1455; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_11; -.
DR Proteomes; UP000000849; 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:UP000000849};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 29..664
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 723..863
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 63..73
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 630..634
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1072 AA; 118698 MW; DC115E0B60774826 CRC64;
MAYPLHRTSH DAGTTVPPSP DLPALEKDVL AHWAADDTFR ASVEQRDAGE NGANEYVFYD
GPPFANGLPH YGHLLTGYAK DVVPRYQTMR GRRVERRFGW DTHGLPAELE AERKLGITDK
SQIDEMGIAA FNDACRESVL TYTKEWEEYV TRQARWVDFD NDYKTLDASF MESVIWAFKQ
LHDKGLAYEG YRVLPYCWRD ETPLSNHELR MDDDVYAARQ DPALTVVLPL VDAPVTLADA
SLLIWTTTPW TLPSNLAVAA GPDIDYVAVR PAEGAFAGRT LVLAASRLAA YARELGESPE
VVTRLTGDDL VGLRYTPPFA YFTGRENAHQ VLAADFVTTE DGTGLVHLAP AFGEDDAAVC
LAAGIATVVP VDSKGRFTTE VPEYAGQQVF DANPGLIREL KERGLVVRHE TYEHSYPHCW
RCRNPLIYKA VSSWFVRVTE FKDRMVELNQ GIEWIPGHIK DGQFGKWLEN ARDWSISRNR
YWGTPIPVWV SDDPAYPRVD VYGSFAELEA DFGRLPLNDK GEPDLHRPFI DELTRPNPDD
PTGRATMRRI PDVLDVWFDS GSMPFAQVHY PFENREWFEH HYPGDFIVEY IGQTRGWFYT
LHVLATAIFD RAAFRNVMCH GIVLGDDGRK ASKSLRNFPD PVLMWDKYGS DAVRWSLMSS
TILRGGNLVV TEEGIRDGVR QVLLPLWSTY YFFTLYAGAA DEGRGYTAQR VTAERAAGLA
PMDRYVLART ADLASSLTAQ LDDYDIPAAC EAVREHLDLL TNWYVRTQRD RFWSEDADAF
DTLWTALEEL TRVMAPLAPL VAEEVWRGLT GGRSVHLADW PATDEALVQD DALVGAMDEV
RAVVSAALGL RKAHQVRVRQ PLRRLTVAVT DPAALAPYTD LLAAELNVKH VDVVEADAAT
AERFGIVQRL AVNARAAGPR LGRAVQHVIK ASRAGAWRVE GETVVVTTDD GDVALEPAEY
ELTTVVGDGT GSDVAAAVLP GGVLVVLDLA LDDALRAEGY ARDVVRAVQD ARKGAGLHVA
DRIALSLQVP AAHVADVEAH REFVAAETLA TSVTVEAADV AEVAVTVARA DA
//
