ID D4AIL9_ARTBC Unreviewed; 975 AA.
AC D4AIL9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=ARB_04114 {ECO:0000313|EMBL:EFE36592.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE36592.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE36592.1}.
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DR EMBL; ABSU01000001; EFE36592.1; -; Genomic_DNA.
DR RefSeq; XP_003017237.1; XM_003017191.1.
DR AlphaFoldDB; D4AIL9; -.
DR STRING; 663331.D4AIL9; -.
DR GeneID; 9522321; -.
DR KEGG; abe:ARB_04114; -.
DR eggNOG; KOG0435; Eukaryota.
DR HOGENOM; CLU_004427_0_0_1; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000008866; 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; cd00812; LeuRS_core; 1.
DR Gene3D; 3.10.20.590; -; 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; 1.
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:UP000008866}.
FT DOMAIN 83..216
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 266..459
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 474..633
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 773..916
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 975 AA; 108491 MW; 5C91A6A4E6F19794 CRC64;
MWVPCAIRGH IRFGGPPTVS HHLLQKFRSL PVRTASTYAN ANQPSKKLDL LAIDKRWKEL
WEGREASVRL MSSSKEKAYV LPMFPYPSGT LHMGHVRVYT ISDVLARFKQ MKGYDVLHPM
GWDAFGLPAE NAAIERGIHP EGWTKQNIAN MRNQLKDLGI RFDWDTEVMT CSPEFYKHTQ
KLFLMLHEKG LAYQAEAVVN YDPVDKTVLA NEQVDSNGCS WRSGAKVEKR ELKQWFFRIT
AFKEALLKDL DSLSGSWPDR ILTMQRHWLG KSRGALVPFT LSIPGETLDI EVFTTRPDTL
HGVQYIALST SHPVVKKMAA NTPGLQEFIN STGSLPPETK AGFKLPGVKA INPIYNLERN
PHLPSSLPVY VAPYVLPDYG EGAVMGVPGH DSRDFGFWKE NSPTEPIVSV VMPLKTGPDS
NDNHGADSAF SGHGQTTDIC GSYSKMPSKT AGEKIINDLK DKGSRARFAE NWRLRDWLIS
RQRYWGAPIP IIHCDSCGAV PVPASQLPVE LPAIPGSQLK DKTGNPLESA DEWLHTECPS
CKGPATRDTD TMDTFVDSSW YFLRFLDPKN NDLPVSPSKS RPVDIYIGGI EHAILHLLYS
RFIFKFLAAE GKIENAADPP EPFLKLLSQG MVHGKTYSDP KTGRFLRPGE VDLSVKGSPV
LTGTQIPANI SFEKMSKSKY NGVDPNTCIE SYGADATRAH VLFSAPVSEV LEWDETKIVG
IQRWFSRIWK AVEDTGNSLK RANFSSAPDA LSSLNDMALP PLGKLSETES NLLLMTDNTI
SSVSYCLEKN QYGLNTVISD LIKLTNAIAA VPLPEESSKT SPSAQSVTPL HTTLYIALNS
LLRMLAPIAP AFASECWEVL HMPLFERVDT VPWVLSSPWP SEFLSESDIK QIRSRGAKTV
AVQVNGKLRF TASVPPFLAN STTPESISNE QEQEWILSHV LRTKEGKVWL QEKNNWDKRK
RVVVVGSGKV INVVF
//
