ID A0A2I1G6N1_9GLOM Unreviewed; 931 AA.
AC A0A2I1G6N1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030520};
GN ORFNames=RhiirA4_340089 {ECO:0000313|EMBL:PKY42297.1};
OS Rhizophagus irregularis.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY42297.1, ECO:0000313|Proteomes:UP000234323};
RN [1] {ECO:0000313|EMBL:PKY42297.1, ECO:0000313|Proteomes:UP000234323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:PKY42297.1,
RC ECO:0000313|Proteomes:UP000234323};
RA Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001372};
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:PKY42297.1}.
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DR EMBL; LLXI01000189; PKY42297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1G6N1; -.
DR VEuPathDB; FungiDB:FUN_013013; -.
DR VEuPathDB; FungiDB:GLOIN_2v1563452; -.
DR VEuPathDB; FungiDB:RhiirA1_197550; -.
DR VEuPathDB; FungiDB:RhiirA1_344301; -.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000234323; 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:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
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:UP000234323}.
FT DOMAIN 72..210
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 258..452
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 466..631
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 670..706
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 759..878
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 931 AA; 108091 MW; FA031285D60D2FC7 CRC64;
MSKIICIYLM LSHLYFNGRV IRTRGFIVFR NKLRFYSEQK NLDLLAIERK WRERWKQLKN
RPKNQENKQK FYILAMFPYP SGMLHMGHVR VYTISDTISR FRKMLGHEVI HPMGWDAFGL
PAENAAIEHG IHPVDWTVSN IKAMKMQMEK ILTDFDWDRE LSTCNSDYYK WTQYLFLKLY
KNGLAYQKEA VVNWDPIDQT VLANEQVDGE GRSWRSGAKV ELRKLKQWFF KITDFAEPLL
KDLDKLNEWP DRVKQMQRYW IGKSEGAEFD FIVNLNRKYR ETTFLIKVFT SRPDTIFGVR
YLAISTDHAL VSKDFLQSDV YSKVLKLAEE MKQYLIGANE KKKSTKGINT GLYATHPITG
ATIPIYVASY VVSDYGTGAV MGVPAHDQRD WNFTKANRIV DEKDIRRVVK PYSAKFIEEC
EVYTSYGILT SDCGQYAGMS SENAINAIVN DAEKRGYGRS AVQYRLRDWL ISRQRYWGAP
IPMIHCSRCN VVPVPESELP VILPTNISLT GRGGSPLKYV KDWLNTKCPK CHGPAERDTD
TMDTFVDSSW YFMRYTDPNN ILLPFSHDKA SKYLPIDVYV GGVEHAILHL LYSRFFTKFL
YKLGMYKPIH NNTQGRDEPF RQLVTQGMVH AKTFKDPLTG RFLKPEEVDL SNPNEPIQKS
TRLAPEISFE KMSKSKYNGI DPEITIEKYG ADATRLHMLY KAPVSEILEW EDSSIVGMQR
WILRVWRLVE SIANFPRQSD DLILNMSMMS NEEKETYRLI NFTIKELTTI FYDTYSFNTA
VSYLIKLTNH LTSISPNVNM SRPVYIYGVK CLVKMMAPMA PSLGEEFWEV LNKGRGTRTI
FEESWPKVDN KGLSVEEVTC IVQINGKMRF SLQVPSSILK DNLMVEMLIR KSNNGQKWIE
ENQTGKKIKR VIHANGGKIV NFVFENNQRK E
//
