ID A0A401L941_ASPAW Unreviewed; 989 AA.
AC A0A401L941;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=AAWM_10897 {ECO:0000313|EMBL:GCB28012.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB28012.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB28012.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB28012.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) 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:GCB28012.1}.
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DR EMBL; BDHI01000029; GCB28012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401L941; -.
DR STRING; 105351.A0A401L941; -.
DR Proteomes; UP000286921; 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:UP000286921}.
FT DOMAIN 88..225
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 275..477
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 491..655
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 801..931
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 989 AA; 110018 MW; E28E0C1C29EBEBD0 CRC64;
MQSLLRFRLS PTRSVLPHPA RWNCASRPIL RPTAVPSRYA TTTASATSIS KKLDLLALDK
KWQERWQTDF LKKPSKTSAD GDAKPKSYIL SMFPYPSGTL HMGHLRVYTI SDVLARFYRM
RGHEVLHPMG WDAFGLPAEN AAIERGIDPA EWTESNITKM KEQLRSISTS FDWDRELATC
APEFYEHTQR IFLMLYEKGL AYQAEALVNY DPVDKTVLAN EQVDANGFSW RSGAKVEKLK
LKQWFFRITD FKEMLLKDLD SLAGGWPERV LSMQRNWLGK SQGAKIKFPV AVNGNNGTDI
DIDVFTTRPD TLYGVEYLAL SLDHPIVLEA AKKDPELRKF LDTAASLPPD SKAGYKLSTV
TASHPLHVID KESPHVARQL PVFAAPYVLS DYGEGAVMGV PGHDARDLAF FRDNVNPDSI
PVVVGPQEEA GADGGDTSIV PSADAKAFTQ EGYLNSLCWK YEGLHSREAK KQIVTDLKQV
GRGDFVEQWR LRDWLISRQR YWGAPIPIIH CGDCGPVPVP DDQLPVKLPK IEGDWLKGKR
GNPLESSHEW VNTKCPSCGG PAKRDTDTMD TFVDSSWYFL RFLDPKNKEQ PFSSSAARPV
DVYIGGVEHA ILHLLYARFI YKFLSQSELF PEIARAGNVA TPFEPFKTLL SQGMVHGRTY
SEPSTGRFLH PSEVDLSSPD KPLIKGTQIT PNVSFEKMSK SKHNGVDPTG CALRYGADTT
RAHVLFSAPV SEVLEWDETK IVGIERWFGR LWKLVNDAQQ SLASFSFTLQ PADLKATSGH
ATGLPSSLQD LSDSDADAVL ATHRTISSVT SCIEKNPYGL NTVISDLTKL TNSLSSSTPS
SPQVLYLSIS SLLRLLSPIA PALASECWEI LNGPVTAGKP STNVPAIFDC PWPTPLLKPE
EADILSARGG QVVAVQINGK LRFTITIPRR LSPTTAPEAS GTVTEEQDWI INRILETDEG
QFWLRKKNDW DKRRRVIVVK GGKLVNVVF
//
