ID E9DS88_METAQ Unreviewed; 962 AA.
AC E9DS88;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 66.
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=MAC_00486 {ECO:0000313|EMBL:EFY93248.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY93248.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY93248.1,
RC ECO:0000313|Proteomes:UP000002499};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(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}.
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DR EMBL; GL698471; EFY93248.1; -; Genomic_DNA.
DR RefSeq; XP_007806826.1; XM_007808635.1.
DR AlphaFoldDB; E9DS88; -.
DR STRING; 655827.E9DS88; -.
DR GeneID; 19244797; -.
DR KEGG; maw:MAC_00486; -.
DR eggNOG; KOG0435; Eukaryota.
DR HOGENOM; CLU_004427_0_0_1; -.
DR InParanoid; E9DS88; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000002499; 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 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-RELATED; 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:UP000002499}.
FT DOMAIN 91..224
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 276..469
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 485..650
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 689..730
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 786..907
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 962 AA; 106714 MW; CCB3F2480DDEB138 CRC64;
MQLVYAKQIG CKGACPALRV ASRWPPGISR PSLIQLPVAP AAASLRRWYA VNLTSLDSKW
RKIWSEADQA GAKQPNSPRT GDRKTNYVLP MFPYPSGSLH LGHLRVYSIA DTVARYHRLK
GDDVLLPMGW DAFGLPAENA ALERGIDPGV WTRRNIKKMK EQLGFMNGSW DWSRELTACD
PEFYKHTQKL FLMLHERGLA YQAEAEVNYD PVDKTVLANE QVDANGCSWR SGAKVEKRKL
KQWFFRTSEY REALLRDLDE LAKNNAWPDR VISQQKNWLG KSTGALVKFP IMAVGGVNVG
NAIEVFTTRP DTLFGVQYVA LAASHPVVAK LAKRDAELQA FLDTLPGLPP DSKVGYLLPH
LRAINPLAYH DETPDATKAS LPIYVAPYVL GDYGEGAVMG VPGHDLRDHS FWKTHQEDQP
VRIVLTASED ESTTTLPMSE PYLEHGVMTH HSGAFKGKRS VEAGQIMVRM LEAANLAKSV
EKWRLRDWLI SRQRYWGTPI PIIHCASCGA VPVPDEDLPV KLPNVEKHWA KGKTGNALES
SPDFVNTSCP KCKGPACRDT DTMDTFVDSS WYFARFIDPH NTQQLFSPEA SKILPVDTYI
GGIEHAILHL LYARFVYKFL ASTSLMPEYT DETASSAEPF KRLITQGMVH GRTFIDPENG
VFLKPDEVDL SDPSSPKIIA TGVPAKVAFE KMSKSKHNGV DPSECIAKYG ADATRAHIIF
QAPVGYILNW DEAKISGVTR WLQRLHDQVV AVAAADESRP AKALLEGKFG SVGSMSSEEL
TQWDADTALW REVQHTIASV TQSYDEVYSL NTIVSDLMRL TNTLAGSQAN EVIKKHACSV
LSRLVAPITP AFADECWSVL HPSKGLIFNA STFPSQDGTL DSAMLQPRQR SCAVQINGKM
RGVVDIPTPP TDLQGDALKD WVVEEILKTE QGKERFGVGK YDLAKAKRVI AVRGGKVMNF
VL
//