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Database: UniProt
Entry: A0A1E4U1C1_PACTA
LinkDB: A0A1E4U1C1_PACTA
Original site: A0A1E4U1C1_PACTA 
ID   A0A1E4U1C1_PACTA        Unreviewed;       919 AA.
AC   A0A1E4U1C1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=PACTADRAFT_83214 {ECO:0000313|EMBL:ODV97801.1};
OS   Pachysolen tannophilus NRRL Y-2460.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Pachysolen.
OX   NCBI_TaxID=669874 {ECO:0000313|EMBL:ODV97801.1, ECO:0000313|Proteomes:UP000094236};
RN   [1] {ECO:0000313|Proteomes:UP000094236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-2460 {ECO:0000313|Proteomes:UP000094236};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-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};
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DR   EMBL; KV454011; ODV97801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4U1C1; -.
DR   STRING; 669874.A0A1E4U1C1; -.
DR   OrthoDB; 5472610at2759; -.
DR   Proteomes; UP000094236; 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; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094236}.
FT   DOMAIN          21..594
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          635..756
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   919 AA;  105128 MW;  D45BC1BFAB85B366 CRC64;
     MMQLGIPLEE ISKFADPTYW LYYFPQLCEK DVTSFGGRVD WRRSMITTDV NPYYDAFVRW
     QMNRMKELGM IKFGERYTIY SVKDGQPCMD HDRQSGEAVL PQEYTAIKIE VVEFAPSAKE
     FFNENKFDTA GKKLYLVAAT LRPETMLGQT CCFVSPNIDY GIFDAGNNEY YICTERAFKN
     MSYQKLTPKR GYFKSVIDIN GKTLIGSKIH APLAVHKELR ILPMETVLAS KGTGVVTCVP
     SDSPDDFITQ KELFHKPEYY GIEKEWAAPE LVPIIKTEKY GEKCAEFLVN ELKIQSPKDS
     IQLAKAKELA YKEGFYNGIM IAGKYKNEKV EVAKPKVKQD LIDSKLAFVY NEPESLVISR
     SGDECIVSLE DQWYTDYGEP NWKQRSLECL HQMNCYTPEV THAFENVFDW LKSWALSRTY
     GLGSKIPWDP KYLVESLSDS TVYHAFYTIN HLLHTDYYGK VIGPLGITSD QMTDEVFDYI
     FCRREDIKSD IPIEKLNILR REFEYFYPLD ISISAKDLIP NHLTFFIYCH TALFQKKFYP
     KAIRSNGHLL LNNAKMSKST GNFMTLEQIV EKFGADASRI ALADAGDSIE DANFDESNAN
     AAILRLTTLK DWSEQIVANI GDLRTGEFNY FDIAFENEMN QLIEETYKQY SLTNYKSALK
     HGLFDYQVSR DYYREAVIVE GMHKDLALRY IETQSLMLQP IAPHFAEYIY REVLGNKEKS
     AQFVAFPKSS KPVSKSIADS LEYVRSLSRS IRETEGAILK KKKGSKTAEV DSKSPVKLTI
     LISSTFPDWQ DQYIELVRES FENHTLNDNS QLKQKINGKD MKRAMPFISL LKQRLTTEPA
     EVVFNRKLSF DEIETVKKVL AILKRSTSIF NCQEIQAISF ASGETVGTDI ITGEKVEIVA
     SPKVIEAAIP GQPGVVITN
//
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