ID X0E1B1_FUSOX Unreviewed; 957 AA.
AC X0E1B1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=FOQG_00428 {ECO:0000313|EMBL:EXL00133.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXL00133.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXL00133.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXL00133.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH658362; EXL00133.1; -; Genomic_DNA.
DR AlphaFoldDB; X0E1B1; -.
DR eggNOG; KOG0435; Eukaryota.
DR HOGENOM; CLU_004427_0_0_1; -.
DR Proteomes; UP000030663; 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 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:UP000030663}.
FT DOMAIN 86..220
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 272..465
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 479..641
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 670..722
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 783..901
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 957 AA; 107033 MW; 67922EB02852D45E CRC64;
MPLLHQRLMS CATARRALSS LSSSSIRHPI IAHTKTATLG AISRRFYAID LTSIDEKWRQ
RWRESNETLK VSEKGTNGQD KHYVLPMFPY PSGTLHLGHL RVYSIADVVA RFRTLRGEKV
MLPMGWDAFG LPAENAAIER GVAPEKWTRS NMAKMKEQLE LMNGSWDWDR ELSTCDPGFY
KHTQKLFLML HERGLAYQAE AEVNWDPVDK TVLANEQVDA NGNSWRSGVK VEKRKLKQWF
FRISEFREAL LEELEALAKE NAWPERVLAQ QKNWLGKSTG ASVKFPVLAM GHDIHAAIEV
FTTRPDTLFG VQYVALAASH PIVAKLAASD PELQAFIDII PGLPADSKVG YLLPHLRAIN
PLAYHEETPD ATKVSLPVYV APYVLGDYGE GAVMGVPGHD LRDNAFWKEH HYDVPVRQVL
SASEDESTTA MKNEPFVEHG VMTEHSGSFK GKNSVAAGEE IVKLLEKADL AKPVEKWRLR
DWLISRQRYW GTPIPIIHCD SCGPVPVPDE QLPVKLPDVD WAETRNGSPL ESSPEFVNTT
CPKCNSPARR DTDTMDTFVD SSWYYARFAD PHNQEQLFSP EAGRTLPVDT YIGGIEHAIL
HLLYSRFIFK FLASTPLLPQ YNEETYKSAE PFKRLITQGM VHGRTYINPD NGRFLKPDEV
DLTDPNQPKV VSSGKTANVS FEKMSKSKYN GVDPSEFISK YGADATRAHM LFQAPVGDVL
NWDEAKISGV TRWLQRLHDQ IVAIAAETAG QTPTAREYLV EKHKSLGSAS TKELKQWDAE
GAIWRHLQRT ITSITTSYEE VYSLNTVVSD LMILTNTLAE NDAASPIVKH EAARALISMM
APITPAFAEE CWVLLCPSAS SIFSSTSFPV PDNSLAELVR PRIQPCAVQV NGKVRGVVDI
PAPPAELSGD ELRDWMVREI LATKEGAARF SEGPYDLRAA KRAIPVRGGK TINFVLK
//
