ID A0A1F6VEA8_9BACT Unreviewed; 1176 AA.
AC A0A1F6VEA8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
GN ORFNames=A2738_03700 {ECO:0000313|EMBL:OGI67924.1};
OS Candidatus Nomurabacteria bacterium RIFCSPHIGHO2_01_FULL_42_15.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801742 {ECO:0000313|EMBL:OGI67924.1, ECO:0000313|Proteomes:UP000178235};
RN [1] {ECO:0000313|EMBL:OGI67924.1, ECO:0000313|Proteomes:UP000178235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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}.
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};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 2 subfamily. {ECO:0000256|ARBA:ARBA00007078}.
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:OGI67924.1}.
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DR EMBL; MFTS01000007; OGI67924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6VEA8; -.
DR Proteomes; UP000178235; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033709; Anticodon_Ile_ABEc.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
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 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; PF00300; His_Phos_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 2.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 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|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035}.
FT DOMAIN 37..521
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 688..824
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 874..1042
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 528..535
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 580
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 1176 AA; 135464 MW; 65217912D91461E3 CRC64;
MAENEENNPV RNNGSQSEPV SNGTSKKSEV ALREEKVLEF WHKNKIFERS LEKKSPKGRY
VFYDGPPFAT GQIHYGHILG STAKDVIGRY RTMQGYYVPR KWGWDCHGLP IENIVEKELG
IAGHVEIEKY GIDKFVEYAR SKVLQYDKDW EKGIERIGRW VDFQGGYKTM DNTFIESVWW
ALSELNKKDL IYEGVRVLAY CPRCETPIAN SEIAMDNSYK DISDISVYVK FELEDEPGTY
LLAWTTTPWT LPGNTAIAIN KNIVYVKVKV ENDVIILAKD TLSNALKNKE YYLLGEIKGE
GLIGKRYIPV FPYYRTSNEA QSKNIWKVWH ADFVTADQGT GLAHEAPAFG EDDMNLAKQN
NIPWIIHVDE TGKFKKEVSD FAGLLVKPKS SEKDGHQKSD IEVIKYLAKN NFLFAKEKII
HPYPHCYRCE TPIIYYALPS WFINIQKEKE NILTQGRSLN WIPAHLKEGR FKNISENAPD
WNISRNRYWA SPLPIWKCDK CKQKTFVSSL KDLKEKTKKS GNKYFVMRHG EAMYNAKHLD
DPKGDPDNHL TKQGEGETVA AAKKLKSEKI DIIFSSPFLR TRETAEILRR ELGFGEEQLI
IDERLHEINE EDQNLVAKRM GDFIYSTEKK FQGKNIIVIS HGNPIWTLQR IVAGVPHADF
SEKQMLNTGE AEELNFIPFP HNANYELDLH RPYIDQVPLV CSCAGSLTRI PEVLDCWFES
GSMPFAQDHY PFKNLEWKKN NFPAAFVAEY IAQTRTWFYY THVVSAILFK QAPFKNIVTT
GTLRAEDGEK MSKSKNNYPD PWIFINKYGV DALRLYLMSS TLMKGEDANF SEKAVQDIAT
KIIGRLFNVF AFYEIYRNKT LEKNDKPRSK NVLDIWILSR FEQILNEITK GMENYDLAEA
TRPIDLFVDD LSTWYLRRSR ERIKEEAANP AREDGARQTL YFVLKTLSKL MAPFAPFTAE
DIWLKLRTGY VPVDGTRHDF AKSDAESVHL ENWPSVSRGI FDIFGNGKSK VLEEMLIARE
ICTIGNAERQ KINIPVRQPL QTLLIKDAAF NLISKNNQIL NLIKEELNIK NIVFDNSVKK
GNKSITLDTN ITPELKQEGD YRELVRALQD MRKKMGLTPS DVVKIVLDTN ETGQKLIEKF
ASDLKKTVLV SQIKFENNDG QEVKIDDLNF KVKIER
//
