ID A0A0V1D5N8_TRIBR Unreviewed; 1040 AA.
AC A0A0V1D5N8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=VHL {ECO:0000313|EMBL:KRY56626.1};
GN ORFNames=T03_11610 {ECO:0000313|EMBL:KRY56626.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY56626.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY56626.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY56626.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRY56626.1}.
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DR EMBL; JYDI01000041; KRY56626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1D5N8; -.
DR STRING; 45882.A0A0V1D5N8; -.
DR Proteomes; UP000054653; 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; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 1.10.730.20; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
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 InterPro; IPR036208; VHL_sf.
DR NCBIfam; TIGR00392; ileS; 1.
DR PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 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 SUPFAM; SSF49468; VHL; 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:UP000054653}.
FT DOMAIN 67..662
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 716..834
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1040 AA; 119621 MW; FB62F5F56AC581BF CRC64;
MEKNVILAFS DFAMRKNLIW FFSTHRQKGI YARTLLLPRS DFPVHMNHEE RVKMDEQIST
ACNVDDLYKW QWNQNKPTFV LHDGPPYANG DVHLGHAVNK ILKDIFARYK AMSGFRVHFR
PGWDCHGLPV ELLAIKSMDE NSRRDPILVR KRAKEFALKA VQSQMDSFKK WAIMADWKNP
YLTLDKEYEG KELEIFKILH QHGLVYRAYR PVYWSPSSRT ALAESELEYV TNHCTEAVYF
KYSVVNFPKK ILALQPTDRI WALVWTTMPW TLAFNNAICF GKKLVYILAK IKSEYYIFAM
DAIDRLRNLL KLEIEVKSTF QGSFLSGLYY ACPMQPDHAL PFYSAEHVTS AKGTGLVHTS
FAHGFEDFAV AVEHGEEVKC FVDEDGRYRR ELGPDLGGLQ VQTEGQAAVL EKFKKYILTK
ENVTQSYPYD WRTKQPVIVR SSKQWFIDTE QLKKAALDQL NDVNFYPANF AQSFKEVLAR
RPAWCISRQR VWGVPVPIFY DPETNEPIES NSLLENTVRL IQQHGSDIWW HSQAGDFAVD
DTTMKLCKSD EILDIWFDSG VSWAAALDEQ RKSSADLIVE GMDQLRGWFQ SLLLTSVAVE
QRSPYKNVLL HGFVLDEQGH KMSKSVGNVI TPDAVISGQG EIGSKQIPAV GVDGLRLWVA
QCAADRTHIP VGPQSLLTVK QTLGQLRSTL CFLLGVLNDF DCSNDSVEYD RLLVVDKYML
HVLAEFQNSM KSAYESFSAL EAVTRAVQFS NGSVSKFYCT TVKDRLYCER AESLKRRSAQ
TVLHEVQTAF TSAVAPLLPY LAEEVHFYRN GKLGSFVFQK GWYDCPQQWT DKTLSDRMDP
LLKARGRFLA DYGKQNTYKF SICINDVSLK ENIALLWSNS ADAVVELADL FRVGQLQIGY
NTNDNEFDVA SVQHPLCSRC RRYICQLLYC TIPPRGFVNV RSYAFHKWIF RDHGTFERLR
CQYYTHTPRF VPPFVFILHP DLSLLRRCVE VVVDQINAGR IQRDDIPGQY LKLIEKTTSR
KIFFQSDVDN TTVKLEKLEH
//
