ID F8P964_SERL9 Unreviewed; 1088 AA.
AC F8P964;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=SERLADRAFT_452911 {ECO:0000313|EMBL:EGO20193.1};
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1] {ECO:0000313|EMBL:EGO20193.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO20193.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "Evolution of plant cell wall degrading machinery underlies the functional
RT diversity of forest fungi.";
RL Submitted (APR-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}.
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DR EMBL; GL945441; EGO20193.1; -; Genomic_DNA.
DR RefSeq; XP_007322938.1; XM_007322876.1.
DR AlphaFoldDB; F8P964; -.
DR GeneID; 18816865; -.
DR KEGG; sla:SERLADRAFT_452911; -.
DR HOGENOM; CLU_004174_1_1_1; -.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000008064; 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 Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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.
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}.
FT DOMAIN 51..120
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 196..763
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 802..924
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1088 AA; 122906 MW; 10669BD21C5BD775 CRC64;
MANTIELAQT GKRDHLKALE KKYQEKWTQE NLFEVNAPSQ EELVGLSVAE IREKYPKWFG
TFPFPYMNGS LHLGHAFTIS KIEFAAGYQR LLGKRVLFPH GFHVTGMPIK ASSDKVIREM
EMFGPDFERF GEETVEEKPS EAVAAPAVVG KATKGKIAAK STGHTYQFQI MESIGVPRSE
IKKFADPYYW LTYFPPICKE DNNSFGSRID WRRSFMTTDA NPFFDAFVRW QINKLHDLGK
IRFGERYTIY SPKDGQPCMD HDRQDGEGHG PQEYTAVKME VVEWSEAAKA EIEGKVGGRK
VFLVAATLRP ETMYGQTNCF VGTAIKYGVF AINQTEAYVC TYRAARNMAF QGISTPRGNI
DQLLELDGIK IVGTKIKAPF AINPEVYVLP MDNVLSTKGT GVVTSVPSDS PDDYQTLVDL
RKKPEFYKID PKWASIDPVP VITTPTYGDL TAPTLVKQLK IQSQKDTKQL AEAKEIAYKE
GFYSGTMLVG EFKGESVQDA KPKVRASMIE SGVALAYAEP EGLVISRSAD ECVVALMDQW
YLDYGEPSWR AQAERLVAKM DTYGSETRNA FEATLGWLNK WACARTYGLG SKLPWDPQFL
VESLSDSTIY MSYYTVAHLL HGGDITGSKL GPLAVTPHQM TDEVWEYIFC NGPWPEPAPL
PREKADKLRH EFNYFYPLDI RSSGKDLVPN HLTFAVYNHA AIFSEDKWPL SMRTNGHLML
NGKKMSKSTG NSLTLRESIE KFGADATRLS LADAGDGVED ANFDEKTANA NILRVHTLLS
WCEEMIKDQA TLRQGPRNSY HDRVFEEEIN DLINITKGHY EATSYKDALK FGFYELQTAR
DWYREVTADI GMHGELVQYW IRIAALLASP IAPHFAEHIW STILQEPKSI QLARWPEPPR
PIDKSVIETG VYMRGTLKMI RDAEVTLMKK INKGKKGKGG EDASFDPKKP RSVRIYVATT
FPEWQNICVQ TVKDSYVEKA EKVDDVKVRE ILIEKGLIKD KRVMPFIQAF KKRMAEFGAQ
TAFRRTLPFS ETEILSEFLP YLKKSLGLVD AEVLSVEEAR THEGEPGFTR SIMDSSEPGS
PAFEYRNV
//
