ID A0A1F6XNJ2_9BACT Unreviewed; 1170 AA.
AC A0A1F6XNJ2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
GN ORFNames=A2917_03480 {ECO:0000313|EMBL:OGI95653.1};
OS Candidatus Nomurabacteria bacterium RIFCSPLOWO2_01_FULL_42_17.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801780 {ECO:0000313|EMBL:OGI95653.1, ECO:0000313|Proteomes:UP000178104};
RN [1] {ECO:0000313|EMBL:OGI95653.1, ECO:0000313|Proteomes:UP000178104}
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:OGI95653.1}.
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DR EMBL; MFVE01000005; OGI95653.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6XNJ2; -.
DR STRING; 1801780.A2917_03480; -.
DR Proteomes; UP000178104; 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; 3.
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; 1.
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 8..494
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 692..830
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 884..1032
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1170 AA; 135286 MW; EB0BE998CC13555D CRC64;
MAKREEAILQ FWKKNKIFQK SLDKNSPKGN YVFYDGPPFA TGLIHYGHIL GSTAKDAVAR
YQTMRGYHVP RKWGWDCHGL PIENIVEKDL NIAGHKEIEK IGIDKFVEHA RSLVLQYDKE
WESGVERIGR WVDFRGGYKT MDNTFIESVW WAFSELNKKG LIYEGVRVLA YCARCETPIA
NSEIAMDNSY KDIADLSIYV KFELENESGT YLLAWTTTPW TLPGNTAIAV NKNITYVKVR
IGNDVLILAK DTLQNVLKEK EYSVVEEIKG SELIGKKYKP VFPYYRNVDL PNKENIWKVW
SADFVTTEKG TGIAHEAPAF GEDDMNLAKQ YSIPWIIHVD ETGRFKPEVT DFSGLKVKPK
DTPEDKDAHM RSDIEIIKYL QKTGAYFDKE KIIHSYPHCM RCDTPIIYYA LPSWFINIQK
VKKNILKRAE SMNWVPAHLK EGRFKNIVEN APDWNVSRNR YWASPLPVWK CEKCTEQVFI
SSLADLKVKT KKSGNKYFVM RHGEAENNAK NIYSSNQKIN HLTEKGRTQV LQTIGHLKSK
KITKIYCSPF LRTRETAQMV AEKIGFPLEK IIYDDRIREL EFGDFSERPV SDYWDYMKDK
IWEFDKKVPG GESFQDGKNR IGNFLYDIDQ KNKNECILII SHGIAVEMVP AVIEAADKKR
SAEVFHLHMK NKTAELHREH EFSPLPHNAN YELDFHRPYI DEIRLVCSCK SEMKRVPEVL
DSWLESGSMP FAQNHYPFEN RDWQKNNFPA GFVAEYIAQT RTWFYYTHVL STILFDHAPF
DNVVTTGTLL SEDGQKISKS KKNYPDPWIF IDKYGVDALR MYLMTSPLMK GEDANFSEKL
VQEISSKIIG RLGNVVSFYE LYPAPEQARY EAGSDVKKSG DILDKWILAR LNQLVSEVTN
GMEAYDMNEA SRPIEGFIED LSVWYLRRSR ERIKDGDKEA KQTLYFLLKT VAKIMAPFAP
FTADDIWLRL KNKNDAESVH LTQWPKMSKP VFDIFGSSQD KILGSMQKVR NIVSLGLEAR
QKAGIKVRQP LARLEIKDFN LGKEYVELIK DELNVKEVKQ NKNLESEVSL DLNITEELKQ
EGDYRELVRA LQDMRKKIGL TPSDVVALTF ETNDMGKELI QKFELDIKKT VLVSEIKFKE
NTGPAFAEGY SEARDEIKID DLVFKVKIEK
//
