ID A0A0S8GVX2_9BACT Unreviewed; 1056 AA.
AC A0A0S8GVX2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
GN ORFNames=AMJ79_04045 {ECO:0000313|EMBL:KPK77171.1};
OS Phycisphaerae bacterium SM23_30.
OC Bacteria; Planctomycetota; Phycisphaerae.
OX NCBI_TaxID=1703411 {ECO:0000313|EMBL:KPK77171.1, ECO:0000313|Proteomes:UP000051901};
RN [1] {ECO:0000313|EMBL:KPK77171.1, ECO:0000313|Proteomes:UP000051901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_30 {ECO:0000313|EMBL:KPK77171.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK77171.1}.
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DR EMBL; LJUC01000040; KPK77171.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8GVX2; -.
DR STRING; 1703411.AMJ79_04045; -.
DR PATRIC; fig|1703411.3.peg.2500; -.
DR Proteomes; UP000051901; 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 ECO:0000313|EMBL:KPK77171.1}; 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 18..635
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 685..838
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1056 AA; 122896 MW; A9BEF3D4BE34B3F2 CRC64;
MFKQVKSACD HIELEHRILK WWEDNQAFEK LRKKNAGNEH WSFLDGPITA NNPMGVHHAW
GRTLKDCYQR YHAMLGHDQR YQNGFDCQGL WVEVEVEKEM GYETKADIER AGLEKFIELC
KARVEKYSKV QTNQSIRLGY WMDWSDSYFT MSDENNYTIW TFLKKCHQRG LIYKGMDAMP
WCPRCETGIS EQERREGYKN VEDVAVFVRF PLQGCEKEYL LIWTTTPWTL AANVAAAVSG
DLTYARVRQN GGVYYLAETL LEVLKEKGGY EVEGTICGKE MIGWEYEGPF DELEIVKRTF
AEAGYTHRVI EWEEVSDAEG TGIVHIAPGC GKEDFDLGKE LNLPVLMPLN EAGIYLDGYG
FLTGKYAGAV AEEVFESLKG KRVYFKHEYY RHDYPHCWRC GTALLFRAVS EWYIDMSWRR
EIMNIVGQIR WIPEWGHDQE LNWLENMHDW MISKKRFWGL ALPIFECECG WFDVIGDQEE
LKERAVEGWE RFEGQSPHRP WVDAVRIKCD KCGKLTCRIT DVGNPWLDAG IVPYSTVKYN
TDREYWGKWV PADLVLECFP GQFRNWFYAL LAMSTMMEDI PPFRTLLGHA LVRDEFGKEM
HKSAGNAIWF DEAVEKMGAD VMRWIFCGHN PINNLNFGYK LGDQVRRRIF STWWNVYSFF
VNYARLDGFD PQRPAVPHDQ LQDIDRWILS KLQALIRLGR ESMENYDVAA VVKAAEDFIE
RLSNWYVRRN RRRYWRPKSE SDQDKLAAYQ TLYQVLADLC KIMAPVAPFI TEEMYQNLVR
SHKTDAPESV HHCDYPQFDD ALYTEGLAEE MDLVADVVSR VLSIREIKQI RVRQPLQRLI
AVTTDERQRK VLKRFEPHLL DELNIKQLEF VESTDQYVSY NVKPNNKNLG PKYGKDLNTI
TELLGRQSAA EIAQKVDGGI NITLQAENKT WELEAQDLIV ESDLPGNLVL SEGEEPALIL
DIAITDPLRR EGWARDIVRH IQQIRKDIGL EIQNHIKIDY QTDDKNLQAA CDEYQDYIRR
ETLCDAMAEY DGLTSTDVKQ VKIGGAALKV FVQKTS
//