ID A0A0V1LMP6_9BILA Unreviewed; 1232 AA.
AC A0A0V1LMP6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00032665};
GN Name=IARS {ECO:0000313|EMBL:KRZ60663.1};
GN ORFNames=T02_12073 {ECO:0000313|EMBL:KRZ60663.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ60663.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ60663.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ60663.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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:KRZ60663.1}.
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DR EMBL; JYDW01000026; KRZ60663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1LMP6; -.
DR STRING; 6335.A0A0V1LMP6; -.
DR Proteomes; UP000054721; 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 CDD; cd00818; IleRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721}.
FT DOMAIN 16..635
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 690..845
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1232 AA; 141950 MW; A0A20DC640D05633 CRC64;
METLHESINF PLEEEKILQL WKKIDAFKTC QERSKGRPIF SFYDGPPFAT GLPHYGHILA
GTIKDTITRF AYQSGFQVER RFGWDCHGLP VEYEIDKTLG LAGPQEIEKF GVSKYNAECR
AIVMRYAKEW QCIVERLGRW IDFKNDYKTL YPSFMESVWW VFKQLYNKGL VYRGVKVMPF
STACGTPLSN FESGQNYKEV IDPAIIVTFP LDEDPSVSLL AWTTTPWTLP SNLALCVNAN
LDYVKIRERS SNRIFILMEA RLNVLYKSEE EYEIIERFHG QSLEGKKYKP LFEYFAHLKT
ECKAFSILCD GYVSAESGTG VVHQAPYFGE DDYRVCLFNH VITKEMNPIC PVDSSGRFTK
EITDFHGQYV KDADKGIIKM LKANGRLIQS STVKHSYPFC WRSDTPLIYK AVPSWFVKVE
FMVEQLLANN EKTYWVPSFV KEKRFANWLQ DARDWAISRN RFWGTPIPLW VSDDGEEVVC
VGSIEELQNL TGKKLEDLHR EYVDVLTIES VTGRGILRRI PEVFDCWFES GSMPYAQKHF
PFENYGEFLR SFPADFIAEG IDQTRGWFYT LLVLSTALFG KPPFKNLIVN GLVLAADGSK
MSKRKKNYPD PMDIVNKYGA DVLRLYLINS PVVRGEFLKF REEGVRDLLK DVFLPWYNAY
RFFFQNVSLY EMKHGKRFTA KLITPTNIMD RWILSFTYNL VAFVKEEMKA YRLYTVVPRL
VKYVNMLTNW YVRMNRKRLK GDFGEEESLI ALETLCQALL LLVRLMASFT PFITEMMWQR
LKTVLDPLAE LKPEDSIHYV KIPDVDRSMI DEDVENHVIT MQSVVEVARV IRDRHALPTK
YPIKEVVLVH HDLRVLDMAQ NMRNYILDEV NARSMMVSVD KAKWGIRSAV DVNLKLLGAR
LKKDLKPVMD ALKAISADDI CSMMELGPIN ILGYEIFREE LQIKYVLGDT DVKDYQAHSD
GRLIVLLNVS QDESMHEEGL AREMVNRIQK LRKKAKLLPQ DDVMIKCELV SGGDSSKVYS
SLCRWREFME QSLKQPIVFL ESPQTESDHL LIIKENVTVK GCVICVCIFS RSAKASQQSS
QLFCPYVDVV DSSGRCVRIL LENPIRTTFC LWNESSITLY KDKLFQQLLV PTDDTKQLNS
TTIYVRAASS SNLPAVTWIN VLIDTTCKAC LTLLNPNQSV TVGLLKAKLK EFFPFLNAQN
IELLDASSKI YKDDTALDVS SIVEQPLLVK CC
//
