ID A0A0B2V9K1_TOXCA Unreviewed; 1148 AA.
AC A0A0B2V9K1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=irs-1 {ECO:0000313|EMBL:KHN78147.1};
GN ORFNames=Tcan_15895 {ECO:0000313|EMBL:KHN78147.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN78147.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN78147.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN78147.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) 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:KHN78147.1}.
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DR EMBL; JPKZ01002155; KHN78147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2V9K1; -.
DR STRING; 6265.A0A0B2V9K1; -.
DR OMA; EIIVIHK; -.
DR Proteomes; UP000031036; 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:UP000031036}.
FT DOMAIN 20..641
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 693..843
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1148 AA; 131973 MW; 021213F523AA8615 CRC64;
MGRLETVPDQ INFSEEEVKT MKRWREQNTF KKSLEMSKDR PRYTFYDGPP FATGLPHYGH
LLAGTIKDVV TRWAHQNGYY VERRFGWDTH GLPVEFEVDK MLGLRGPRDV LEMGIDKYNG
ECRKIVMRYS SEWEEAVERM GRWIDFRHDY KTLYPWFMES VWWAFSQLFK KGLVYRGVKV
MPFSTSCSTP LSNFEAGQNY KDVVDPAVVI GFTLDEDSSI QLAAWTTTPW TLPSNLCIAV
HPDLQYVTIR DRATQKKYIL MEERLCELYK NSDTYEVLDR YKGEALKGKT YQPLFPYFAH
LKKELGAFRV LTASFVTTDQ GTGVVHQAPY FGEVDYQTCL ENGVITRDMK AICPVDECGK
FQEEVTDFKG MYVKDADKHI CRYLKEHGNL IKHGEVKHSY PFCWRSDTPL LYMAVPSWFI
RVEAIVPYLL DNNDKTYWVP SFVKEKRFAN WLRDARDWAV SRNRFWGTPI NLWVSDDLEE
IVCPASIAEL ELLTGTKITD LHRESVDRLT IPSKTGRGEL HRVSEVFDCW FESGSMPYAQ
NHYPFENRKV FEENFPADFI AEGIDQTRGW FYTLLVLSTA LFNRPPFKNL ICNGLILASD
GSKMSKRKKN YPDPMEIVRK YGADALRVYL VNSPVVRGEN LRFREEGVKD VLKDVLLPWY
NAYRFFVQNV QLFEHNFGKE FTLVECESAN VMDRWILSFS NSLVTFVRKE MEQYHLYAVV
SPLTKFFDTL TNCYIRLNRK RIKGEGDEED REHALSTLGR VLLLTVRLMA PLTPFFCDLL
WQNLRHIVTS PSESVHFEMI PQPRSDLIDE SVERRVAAMR AVVDLVRVVR ERKSIPVKYP
LKEMVVINRD SQFLEDLVSL EAYILSELNI RKMTVSQDKA KYGVHLKAEP NFRLLGARLK
GDQKKVADYL KNKVSEEELT SFLERGTLNV LGHDLTTEEV TVSYCTSGDS SSSGHFETNS
DSQTIVMLDT SEDESLIEEG LAREVTNRIQ KLRKSAKLVS TDEAFVYCKV TPPSHQLRAV
MLSHAKQIRE ATGTAFELGD LPADRSASAT SSSSVKDAQL ELVLVVENNN NAAPAITVHY
GSQSRKVQLA SGDALLTYTA LMYEVRALFS LWSSHRLLLS LVEPPAKQII SASDNLMDLA
GKSLYVLT
//
