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Database: UniProt
Entry: A0A0S8GVX2_9BACT
LinkDB: A0A0S8GVX2_9BACT
Original site: A0A0S8GVX2_9BACT 
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
//
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