ID A0A094EL43_9PEZI Unreviewed; 1124 AA.
AC A0A094EL43;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=V499_03383 {ECO:0000313|EMBL:KFY77178.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY77178.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY77178.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY77178.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 -!- 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:KFY77178.1}.
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DR EMBL; JPKB01000524; KFY77178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EL43; -.
DR HOGENOM; CLU_004174_1_1_1; -.
DR Proteomes; UP000029295; 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 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}.
FT DOMAIN 66..135
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 223..798
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 837..966
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 151..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1124 AA; 126025 MW; EE0C5B8D5183867F CRC64;
MAASDAAAKA LDDLHLSKTK ELKGTEKRDS LIAVEKKYQK KWQDDAVFQP NAPSIADIPL
SALSAKEVRE KHPKFFGTMA YPYMNGTLHA GHSFSVSKIE FTAGWARMQG KRALFPMGFH
CTGMPIKACA DKLINEIKLF GKDFSGYSEE DEASDKLKEK SPPAPTSARE DVTKFTAKKG
KAAAKVVKMK YQFQIMRAQG IPNEQIHEFA DPNHWLDFFP PLCKQDLTNF GCRIDWRRSF
VTTDANPYYD SFIRWQMNRL RELKKIKYGK RYTIYSPKDG QPCMDHDRSE GEAVGPQEYT
ALKLKVLEWA PEAKKAVADK LPQGADAFFV PATLRPETMY GQNCCFVGPK ITYGVYKVSE
KEYYIITERA ARNMAYQGVF PVNGVYEKVA EVTGADCVGT LVNAPLSIHT EGIRILPMDS
VLPTKGTGVV TCVPSDSPDD FATITDLAKK AEYYGIKKEW AELEIIPIID TPSYGNLTAP
FLVKKLKIAS PKDTKQLEEA KELAYKEGYY QGTMCYGPFT GEKVEDAKPK VRQQLLDSGG
AFAYSEPEKR VVSRSGDDCC VALMDQWYLD YGEESWRKVA LQHVDNADGN GLNTYSQETK
NGFEGVLNWL NQWACARSFG LGSKLPWDPQ FLVESLSDST IYMAYYTVAH LLHGDIFGRT
PGLLKDLTPE QMTDEVWDYI FARREVSEDV LQSKISLEGL ETMRREFEYW YPLDLRVSGK
DLIPNHLTFF IYIHIALFPP EYWPKGVRAN GHLTLNGEKM SKSTGNFMTL DEMVKKYGAD
ASRIALADAG DGVADANFEE DVADNNVLRL FTLREWIEEQ VKEQETLRTG EKNDFLDRLF
DNEMNAIARE AKGHFDDTNY KLALKSGLYD FIGARDFYRE ASTAAGIKMH KDLVFKYIEL
QALLLAVIAP HWSEYIWLEV LNKSATVQDA LFPEIPAPDA SLSAMREYVR TTASNITSAE
AAQQKKKAKG KDISFDPKKP KKLTIFAAKS FPAWQEKYID LVREVFDPAT KAFNDKELTP
KISKMGEMKK AMPFVQGLKK RLTGGEQPET VFDRKLAFDE SKTLLQMVPG LKKAAGLKIV
DIVEVAEGGA TGVLVGGGEV ASLPPPAAGA VPGVPTFHFE NVEE
//
