ID A0A3N4MGN1_9PEZI Unreviewed; 1123 AA.
AC A0A3N4MGN1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-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=L211DRAFT_833987 {ECO:0000313|EMBL:RPB27975.1};
OS Terfezia boudieri ATCC MYA-4762.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pezizaceae; Terfezia.
OX NCBI_TaxID=1051890 {ECO:0000313|EMBL:RPB27975.1, ECO:0000313|Proteomes:UP000267821};
RN [1] {ECO:0000313|EMBL:RPB27975.1, ECO:0000313|Proteomes:UP000267821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4762 {ECO:0000313|EMBL:RPB27975.1,
RC ECO:0000313|Proteomes:UP000267821};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
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 ---------------------------------------------------------------------------
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; ML121530; RPB27975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4MGN1; -.
DR STRING; 1051890.A0A3N4MGN1; -.
DR InParanoid; A0A3N4MGN1; -.
DR Proteomes; UP000267821; 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; 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:RPB27975.1}; 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:UP000267821}.
FT DOMAIN 62..129
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 213..785
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 826..947
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1082..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 127254 MW; 75AC6C2F859109D7 CRC64;
MVSVEALDPA NASKNTLKLE NTEKRDTLIA IERKYQKYWS DNGLFEIDAP TLEENPTTDP
EELRKKHPKF FATMAYPYMN GTLHAGHSFT LSKVEFQTGF ARMEGRRALF PLGFHCTGMP
IKACADKLVR EIEMFGKNFE GYKEEEVEEE EPIPIAAAGK NDPTKFAAKK GKAVAKAVRL
KYQFQIMKAL GLPQEEVHKF ADPLHWLEFF PPLCKQHCTN FGLRIDWRRS FITTDANPYY
DAFVRWQMNR LKELGKIKFG ERYTIYSPRD GQPCMDHDRS DGEGVGPQEY TGIKLKVLEF
AEEAKAAVEG KIPADANVYM VAATLRPETM YGQTCCFVGP RIQYGVFRVS EKEYFIITER
AARNMAFQGV FENRGEYPSV ATLNGQSLIG TKVHAPLSVY TEGIRVLPME TVLATKGTGV
VTSVPSDSPD DYATVTELAK KADYYKIKKE WVDLPIVPII RTPSYGDKTA EFLVKQLKIN
SPKDTKQLAE AKELAYKEGF YLGTMIIGDF KDEEVQAAKP KVRGQLIKKG EAIAYSEPEG
QVMSRSGDPC IVALCDQWYL DYGEAEWRKA TEGHVADTLN TFYPETKHGF EATLAWLNQW
ACARSYGLGS KLPWDPQFLV ESLSDSTIYM AYYTIAHYLH SSIDGKEIGP AGVKAEQMID
EVWDYIFCRR ELSPDVIKAS GIPKETLQKF RREFEYFYPL DCRVSGKDLI QNHLTFFLYC
HVALFPPQYW PRGVRANGHL MLNGEKMSKS TGNFLTLDET VKKFGADASR IALADAGDGI
EDANLEESVA NAAILRLYNL KEWCEEVVKM GNEGQLREGP KDSFWDRVFE NEMNDLVLKT
RVQYERTMFK LALKEGFYEF QAARDSYREA CTAANIGMHK ELVFRFIEWQ ALMITPIAPH
WAEYIWQELL GKKISIQCAL YPEPTAPISV PLTGALDYVR TISTKITSTE AAQLKKVGKG
KAISYDPKKP KRLSIYVALS YPTWQDKYIE LVRRHFDAFT VTINEAELKP VIVKMGEMKK
AMPFVQNLKQ RLVFQKEDPK TVFDRKLVFD EVKTLGEVLA VLKRSTGCKE VEVIVVEEGG
RKGKRVPDEG RGNWEDGLVM EGLSGPSESA TPGNPGFAFE NVE
//
