ID A0A2W1ZRW2_9MICO Unreviewed; 1088 AA.
AC A0A2W1ZRW2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=DEJ23_12880 {ECO:0000313|EMBL:PZF55037.1};
OS Curtobacterium sp. MCSS17_008.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=2175647 {ECO:0000313|EMBL:PZF55037.1, ECO:0000313|Proteomes:UP000248620};
RN [1] {ECO:0000313|EMBL:PZF55037.1, ECO:0000313|Proteomes:UP000248620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCSS17_008 {ECO:0000313|EMBL:PZF55037.1,
RC ECO:0000313|Proteomes:UP000248620};
RA Chase A.B., Gomez-Lunar Z., Lopez A.E., Li J., Allison S.D., Martiny A.C.,
RA Martiny J.B.H.;
RT "Emergence of Soil Bacterial Ecotypes Along a Climate Gradient.";
RL Submitted (JUN-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=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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PZF55037.1}.
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DR EMBL; QKSM01000014; PZF55037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1ZRW2; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000248620; Unassembled WGS sequence.
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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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:UP000248620};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 29..678
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 732..868
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 59..69
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 644..648
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1088 AA; 120647 MW; 663E458FFF0AE29B CRC64;
MRYPLNRPAD DTAAGVTPSP SFPAVEQGIL AFWKGDDTFQ ASIDQREGCP EWTFYDGPPF
ANGLPHYGHL LTGYAKDVFP RYQTMRGKQV HRRFGWDTHG LPAELEAMRQ LGITEKHEID
DMGVDVFNAA AKKSVLQYTD EWQAYVTRQA RWVDFEDDYK TLDVTFMESV LWAWKQLWDK
GLAYEGFRVL PYCWNDQTPL SNHELRMDDD VYKMRQDQSV TVAFPLRGTR ADELGVTGVR
ALAWTTTPWT LPTNAALAVG PEIAYAVVPA GPGGAADGGE AGSARYLLAS DTVAAHAKDL
GYESADDALA AVLRTVAGAE LDNVEYERLF DFLADQEGYE HAWRILVAEY VETGEGTGIV
HQAPAYGADD QEVCAAAGIP VVLSLDEGGV FTSQFGDVAG MLWSDANKPL TKAVRDTGRL
LRQASYEHSY PHCWRCRKPL IYKAVSSWFV RVTEFRDRMG ELNQDINWVP DNVKDGQFGK
WVGNAIDWSV SRNRYFGTPI PVWQSDDPEF PRTDVYGSLE ELERDFGRLP LNADGEVDLH
RPFIDDLTRP NPDDPSGKAT MRRISDVFDV WFDSGSMPYA QVHYPFENRE WFEEHSPADF
IVEYIGQTRG WFYVMHALST ALFDRPAFRN VISHGIVLGS DGQKMSKSLR NYPDVSEVFD
RDGADAMRWF LMSSSVIRGG NLVVTEEGIR QGVREFLLPL WSTYYFFTLY SNASGASGYQ
ATRRTDSTDV LDRYLLAKTR VLVTDVTTHL DALDTPLAAQ AVRDFADVLT NWYVRRSRDK
FWLGAESSPD ARAAFDTLYT VLETLTRVAA PLAPLVTEEV WKGLTGGRSV HLEDFPEPDE
FPADDALVAA MDRVRDVASK GLALRKATGR RVRLPLATLT LVVPDPAGVE PFADILRDEL
NVKQVVLEQQ EESSLGRYGI ERKLTVNARA AGPRIGKQVQ QVIPAAKKGD WVATESGVTV
GGVDLVEGEY TLDLTVADDS VAVAFLDGGG FAVLDTVTTP ELEAEGLARD VVRAVQQARR
DANLDVSDRI VLTLRVSEDA HGPVRAHEQL IAGETLATSV EVTTTTFAPG EGSDVGDGAK
VSVEVARA
//
