ID A0A1G1ZKH6_9BACT Unreviewed; 1148 AA.
AC A0A1G1ZKH6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
GN ORFNames=A3E64_01595 {ECO:0000313|EMBL:OGY65128.1};
OS Candidatus Harrisonbacteria bacterium RIFCSPHIGHO2_12_FULL_48_16.
OC Bacteria; Candidatus Harrisonbacteria.
OX NCBI_TaxID=1798405 {ECO:0000313|EMBL:OGY65128.1, ECO:0000313|Proteomes:UP000177174};
RN [1] {ECO:0000313|EMBL:OGY65128.1, ECO:0000313|Proteomes:UP000177174}
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 -!- 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:OGY65128.1}.
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DR EMBL; MHJH01000003; OGY65128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1ZKH6; -.
DR STRING; 1798405.A3E64_01595; -.
DR Proteomes; UP000177174; 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:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.620; HUPs; 3.
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; IPR002300; aa-tRNA-synth_Ia.
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.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 16..504
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 692..824
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 873..1008
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT BINDING 501..508
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 556
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 1148 AA; 132445 MW; C4BDD48B457F86CD CRC64;
MLNKLKQFNL PELEEKILKF WKENNVFRKS VALRQAQGKK AKPFRFFEGP PTANGRPGIH
HVLARSFKDV ILRYKTMRGH FVLRRAGWDT HGLPVELEVE KKLGIKNKRE IEKFGIAEFN
TQAKMSVWAY KSEWERLTER IGFWLDFGNP YVTYENKYVE SLWWVFSEIS KRGFLKKLYK
VIPWCPRCQT PLSSHELGQP GAYKLTKDPS VYVKFEIRNS KSLPRRQAGE TRKKQKEFLL
VWTTTPWTLP GNVAVAVNSK LTYTKYKIGD EYVWSYNVPP KLEGKEVEVV EKMSGQKLVG
KEYEPTYPNK GEHKVIAADF VSTTEGTGLV HIAPAYGEDD LRVAGKGETP ITIDDRGFMK
KGLPGGGKFI KEADKDIISD LAKRKILYSS GTIEHEYPFC WRCSTPLIYF ARVAWFLEMS
RLREEMLKAN QKINWIPEHI KEGRFGEWLR DIKDWAISRE RYWGTPLPIW ECGKCRHQKV
VGSLDELGEK SYSQNNYFIM RHAESDHNLK DIIASGPENG KNVSKLTAKG RLQMEKSAQT
LKREKPDLII CSPYARTRET AKIVSKITGA KVITDKRLEE LNTGVFNGRP ISEHRKFFSN
RMESFTKAPA GGESLNDVKR RMMDFLKETD SQYQNKNIVI VSHGDPLWVL DGAVRGLSNE
EILKQDYYLE VGKWSKLPFP NWPFNHDGEV DLHRPFVDEV YLRCSECGSK MERVKEVADV
WFDSGAMPFA QWHYPFENKK LIDGGAQYPA DYIAEGIDQT RGWFYTLLAV ATLLKRDLPY
RNVISLGLLL DKTGQKMSKS KGNVVDPWQM LQKYGADVLR WYFYTVNPPG EPKRFDENDL
RKTLNKLFML LYNSFVFYST YGKEKHKPIK VLDEWIIDRL NATADMVTAN LEVYAIGDAA
QEIEALVDDL SRWYIRRSRK NVSGKTLRLV LSGIAKMMAP FAPFFAEALW LSLGNKDSVH
LQDWTSMRSK SKVKSSKLLT AMAEVRRLAS LALAEREKAG IKVRQPLREL RIKPCLPAGR
NKELEKNKEL LNLLADEVNI KEVVLDNKIN GEIQLDTTLT PELRNEGILR ELVRMVQGLR
HDAKYQPHDK IILMMELPKE LLKVVDANSR ELKMAVNAKN VVFKKEKFDA ELNTKLENAP
VWIAVKKF
//
