ID W9CML2_SCLBF Unreviewed; 1124 AA.
AC W9CML2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=SBOR_3867 {ECO:0000313|EMBL:ESZ95760.1};
OS Sclerotinia borealis (strain F-4128).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ95760.1, ECO:0000313|Proteomes:UP000019487};
RN [1] {ECO:0000313|EMBL:ESZ95760.1, ECO:0000313|Proteomes:UP000019487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT pathogenic fungus.";
RL Genome Announc. 2:E0117513-E0117513(2014).
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 -!- 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:ESZ95760.1}.
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; AYSA01000166; ESZ95760.1; -; Genomic_DNA.
DR AlphaFoldDB; W9CML2; -.
DR STRING; 1432307.W9CML2; -.
DR HOGENOM; CLU_004174_1_1_1; -.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000019487; 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; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; TIGR00395; leuS_arch; 1.
DR PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
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.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:ESZ95760.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000019487}.
FT DOMAIN 67..135
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 212..791
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 832..960
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1124 AA; 126714 MW; 913B80C6A0E18210 CRC64;
MAAVEATAKA LENATISKTK ELKGTEKRDK LIAIERKYQA QWEKDGIFQP DAPSTSEIPL
HSVSAAELRE QHPKFFGTMA YPYMNGTLHA GHSFTVSKVE FTAGFARMQG KRTLFPMGFH
LTGLPIKACA DKLVNEIKLF GKNFENYKEE EELEEKTNIS APSTHHEDVT KFTAKKGKAA
AKVIKMKYQF QIMRALGIPM EDIYQFADPQ YWGAYFSPLC KRDLTNFGAR IDWRRSFVTT
DANPYYDSFV RWQMNRLKEL KKIKFGKRYT IYSPKDGQPC MDHDRSDGEG VGPQDYLAMK
LKVMEWAPEA ADAIKGKLPA DADVFFVAAT LRPETMYGQN CCFVGPKITY GVFKVSKNTY
FVITDRAARN MSYQNIFPGN GTVDKVAVIT GSACVGTLVH APLSVHKDGV RILPMESVLP
TKGTGVVTCV PSDSPDDYAT IMDLAKKADY YGIKKEWAEL EIISVITTPS YGDMCAPFLV
NKLKIASPKD KTKLEEAKEL AYKEGYYQGT MSFGEFKGEK VEVTKPKVRK QIIDACQGFA
YSEPERKVTS RSGDECCVAL MDQWYLDYGE ESWRKIALEY VDSGLNTYSQ ETKNGFEGVL
NWLNQWACAR TYGLGSKLPW DPQFLVESLS DSTIYMAYYT IAHYLHNDIF GKTPGLAGIK
PEQMTDEIWD YVFARRDISD DILNDSKIPQ DTLASMRREF EYWYPLDLRV SGKDLIPNHL
TFFLYIHIAI FPPEYWPKAI RANGHLLLNG EKMSKSTGNF MTLFDMINKY GADASRIALA
DAGDGVADAN FEEDVADNNV LRLFTLREWC EDMVKDQDSL RTGEKTDFLD ALFENEMNAI
VHECRQHYEA TDFKLALKSA LYDFTAARDF YREASIAAGI KMHKDLILQY IELQALLLTV
IAPHWSEYIW LEVLHKTTTI QNALYPTVPA PIPALSAARD YVRSTSSNIT SAEAAQQKKK
AKGKDIGYDL KKPKKLTIFS AAKFPAWQQK YIDLVRESWN PETKSANDKE LNGKIAKMGE
MKKAMPFVQT LKRSLQGGEV PDQVFERKLA FDEKQTLKNM VPGLKKAAGL AVIEVVIVDG
DEGGKKGVIV SVEGSEEKEY GALPIMAEQA VPGFPTFLFE NVEV
//
