ID A0A168GDA7_CORDF Unreviewed; 1070 AA.
AC A0A168GDA7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-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 ORFNames=LEL_06024 {ECO:0000313|EMBL:OAA76340.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA76340.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA76340.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA76340.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA76340.1}.
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DR EMBL; AZHF01000004; OAA76340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168GDA7; -.
DR STRING; 1081108.A0A168GDA7; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000076881; 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:UP000076881}.
FT DOMAIN 12..634
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 691..846
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1070 AA; 123542 MW; FEB432E783A68AD6 CRC64;
MSIDFPKEEE IVLEKWKEIN AFHRQLELTA TLPRYTFYDG PPFATGLPHY GHLLASTIKD
IIPRYWAMKG YHVERRFGWD THGLPIEHEI DKKLGISGKA AVTELGIGKY NEECRAIVMR
YASEWRATIE RLGRWIDFDN DYKTMDPTFM ETLWWVFKQL FDKGSVYQGY RVMPYSTVLT
TALSNFEANQ NYQDVTDPAV VVSFPLLDDP NVNLLAWTTT PWTLPSHTGL AAHPDFEYIK
IQDGKSGKMY ILLEKLLTTL YKDPKKADFK IIARIKGKDM LGWRYEPLFD YFYEEFKDKG
FCVLNATYVT ADSGVGIVHQ APAYGEDDYN IALEAGIISE KRPPPDPIND TAHFTERVRD
FAGMHVKEAD KHIIKYLKNS GRLVVESQIR HSYPMCPRSD TPLIYRAVPS WFIRIPEIVP
DMLKNIEGSH WVPSFVKEKR FASWIANARD WNVGRNRYWG TPIPLWVSDD LEERVCIGSV
EELRKLSGHE DEITDLHRDK IDHITIPSKM GKGVLRRVDE VFDCWFESGS MPYASQHYPF
ENVDKFNASF PGDFIAEGLD QTRGWFYTLL VLGTHLFGKS PFQNCVVNGI VLAEDGKKMS
KRLKNYPDPA IVMQKYGSDA LRLYLINSPV VRAEPLRFKE SGVKEVVQKV LLPLWNSYKF
FEGQVALLKK VEGVDYMWNP DLESTNTNVM DRWILASCQS LLEFVNKEMT GYRLYTVVPR
LLELIDNTTN WYIRFNRRRL KGENGLDDTQ HALNALFEVL FTLCRGLAPF TPFLTDNIYS
RLLPHIPKSL QAEDPRSVHF LRFPDVRSEL FDSAVERRVS RMQRVIELAR VSRERRSIGL
KTPLKTLVVL HHDQQYLDDV KSLENYITEE LNVRDLVLTS DEDKYGVQYS VTADWPVLGK
KLKKDMARVK KALPSLTSEQ CQGYVRDKQI LVDGIKLEEG DLVVRRGVKE DETSKTWETN
TDSDVLTLLD VHIYQGLAQE GLAREVINRV QKLRKKAGLQ QTDDVKMEYR MLSDPESIGL
EDVLGTQSAA FEKVLRRPLD KHEDGVTGEV IAEEEQEIQR ATWMLRLLKL
//
