ID A0A1J5H762_9BACT Unreviewed; 995 AA.
AC A0A1J5H762;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
GN ORFNames=AUK07_00560 {ECO:0000313|EMBL:OIP75894.1};
OS Parcubacteria group bacterium CG2_30_36_21.
OC Bacteria.
OX NCBI_TaxID=1805315 {ECO:0000313|EMBL:OIP75894.1, ECO:0000313|Proteomes:UP000183564};
RN [1] {ECO:0000313|EMBL:OIP75894.1, ECO:0000313|Proteomes:UP000183564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_36_21 {ECO:0000313|EMBL:OIP75894.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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 -!- 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:OIP75894.1}.
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DR EMBL; MNZD01000009; OIP75894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5H762; -.
DR STRING; 1805315.AUK07_00560; -.
DR Proteomes; UP000183564; Unassembled WGS sequence.
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 Gene3D; 3.40.50.620; HUPs; 2.
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.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OIP75894.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 11..632
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 685..831
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 995 AA; 116143 MW; BD7F64B34C8E66A7 CRC64;
MTINFPEMEQ KILKFWQENK IFEKLRNKNQ GKKRWSFLDG PITANNPMGV HHAWGRTYKD
LFQRHKAMQG FDQRFQNGFD CQGLWVEVEV EKELGFKDKK DIEKYGIEKF IQKCKDRALK
YSAIQTKQSI RLGQWMDWEN SYYTMSDENN YAIWHFLKRC QEKGLLYKGR DVVPWCPRCG
TAISQHEILT EEYQEICHKS VFVKLPVVGQ KNTFFLAWTT TPWTLPANVA LAVHPDLEYA
KIKDGKENIF ILLKDKSELI PDGKIIETFK GKKLEGIKYQ GMFDELPEVK ETLKNYKHAV
ILWDGVSPEE GTGIVHTAPG CGQEDFHLAK ELKIPVVNPI NPTDDESRYK AGFGLLSGKL
VTEVNDLIFE DLIKKSLVFK IENYTHRYPT CWRCKTELIF RLVDEWYISM GKLREGLMKS
AQKIKWIPPF GLERELDWLK NMQDWLISKK RYWGLALPIY ECSKCGSFEI IGSKKELKEK
AVEGWEEFAA PLKRGGHSPH RPWVDKVKIR CSKCGEIISR IPDVGNPWLD AGIVSFSTIK
YFSDKEFWQK WFPIDFISES FPGQFKNWFY SLLVMSQVLE NCPPMKTIFG YAMVVDEKGE
EMHKSKGNAI WFDEAVEKIG ADVMRWMYAK QNPVCNLRFG YKAAEETRRK LLTLWNSYAF
FETYVSKNEF PISNNQFPNF KSLLDKWILS RLNGLIKKVT ESLDDYDASR ASLAIENFFI
NDLSLWYIRR SRKRFRETKK EAVATLYFVL LNLAKLIAPI MPFFSEEVYQ KISNSQFLIS
NSVHLEDWPK VDKKLINKKL EKKMEKVREI VALALAERAK VGIKVRQPLS KLKVKSQKLK
VKSQKLKVKS QKLKVENELI HLIKDEINVK EIVFDSKIKG EVELDTEITP QLKEEGIIRE
VIRQIQEMRK KAGLKPKDKI LVRYLGSSDL NKILVKNKNF ILKEAKIKNL ILGLRPPHHP
PAKGGPPEKL KETFDVEKKI KVDQEKLYLA IKKLE
//
