ID R9AJR3_WALI9 Unreviewed; 1082 AA.
AC R9AJR3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 ORFNames=J056_001152 {ECO:0000313|EMBL:EOR00266.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR00266.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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}.
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DR EMBL; KE007236; EOR00266.1; -; Genomic_DNA.
DR RefSeq; XP_009269055.1; XM_009270780.1.
DR AlphaFoldDB; R9AJR3; -.
DR STRING; 1299270.R9AJR3; -.
DR GeneID; 20374104; -.
DR KEGG; wic:J056_001152; -.
DR eggNOG; KOG0434; Eukaryota.
DR HOGENOM; CLU_001493_1_1_1; -.
DR OMA; EIIVIHK; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000014064; 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:UP000014064}.
FT DOMAIN 26..647
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 703..860
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1082 AA; 124348 MW; 3C55F94CEED3B044 CRC64;
MSRDSKDFGS YEINSQFNFP VEESKVLAYW RDIDAFRTQL KHSEGKQTFS FYDGPPFATG
LPHYGHLLAG TVKDIVTRHA ASSGYHVPRR FGWDCHGLPV EHEIDKKLGI SGREDVLNMG
IDKYNEECRA IVMRYSAEWR NTVERMGRWI DFDHDYKTLN TSFMESVWWA FGELFNKDLV
YRGLRVMPYS TACTTPLSNF EAGQAYKDVS DPAVVVSFPL VNDPSTSFLA WTTTPWTLPS
NLALCVNPSH TYLKIHDEEK NRDFIIHEKL LTTLYKDPKK AKFQKVAQYK GSDMKGWKYE
PLFNYFYDEF KDVAFQVLND DYVSADAGTG IVHQAPAFGD DDHRIAIANG IITPDQMPPC
PVDDSGKYTE RVSDYKGVHV KEADKDIQKY LKSINRLIVQ STINHSYPFC WRSGTPLIYK
AIPVWFVKVS QITNDLIENN KETRWVPANI GENRFGNWLQ NARDWNVSRN RYWGTPMPLW
VSEDYEEIVA ISSIEQLEQL SGVSNISDIH RDKIDHITIP SKKGKGVLKR VDEVFDCWFE
SGSMPYAQAH YPFENKEEFE KSFPADFVSE GLDQTRGWFY TLLVLGTHLL GKAPWKNLIV
TGLVLAADGK KMSKSLKNYP DPNHIIDKYG ADAVRMFLVN SPIVRGDNLR FREEGVKEVT
SRVMLPWLNS FRFFLGQAAL AKKEQGIEFM YDASAPRSEN LMDRWVLARC QSLIKIVKEE
MAAYRLYTVI PRLLSLIDEL TNWYIRFNRR RLKGENGKED TIAALRTLFE ALFTLCRTMS
SFTPFITENL YQGLRPFIGD NIPGATDTRS VHFLPFPDVR EDYFDSVIER RVSRMQNVIE
LGRVIRERKR IAVKTPLKTL IVFHHKEEYL SDVRHLEGYI KEELNVRELV VTSEEEFIGI
KYKVSADWPV LGRKLRKDMP RVKNNLPKVS NDDAKGYMQN GKLTVDGIEL QAGDLTVQHY
VDLPESMEGF EPISDSNITI VLDYRLHPEL ESEGLAREFI NRIQRLRKKA NLLQIQDVDV
VVKYLGEDGD ISGLQNAIEM HKDTIVRSTK SNPLSDKENA QVIATEDQEI GAVKFNLTLV
GA
//
