ID A0A167DYF8_9ASCO Unreviewed; 1049 AA.
AC A0A167DYF8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 Name=CDC60 {ECO:0000313|EMBL:ANB13442.1};
GN ORFNames=AWJ20_1733 {ECO:0000313|EMBL:ANB13442.1};
OS Sugiyamaella lignohabitans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Sugiyamaella.
OX NCBI_TaxID=796027 {ECO:0000313|EMBL:ANB13442.1, ECO:0000313|Proteomes:UP000189580};
RN [1] {ECO:0000313|EMBL:ANB13442.1, ECO:0000313|Proteomes:UP000189580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10342 {ECO:0000313|EMBL:ANB13442.1,
RC ECO:0000313|Proteomes:UP000189580};
RA Bellasio M., Peymann A., Valli M., Sipitzky M., Graf A., Sauer M., Marx H.,
RA Mattanovich D.;
RT "Complete genome sequence and transcriptome regulation of the pentose
RT utilising yeast Sugiyamaella lignohabitans.";
RL Submitted (FEB-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; CP014501; ANB13442.1; -; Genomic_DNA.
DR RefSeq; XP_018735919.1; XM_018878636.1.
DR AlphaFoldDB; A0A167DYF8; -.
DR GeneID; 30033568; -.
DR KEGG; slb:AWJ20_1733; -.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000189580; Chromosome a.
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, ECO:0000313|EMBL:ANB13442.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000189580}.
FT DOMAIN 4..55
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 140..718
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 761..886
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 77..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1049 AA; 119140 MW; 7296D7C7EECEE93D CRC64;
MAYPYMNGVL HAGHCFTLSK VEFATGYERM LGKNALFPLG FHCTGMPIKA CADKLTREIE
QFGENFENAP TPEEEAAVAA AAEEAEKSKK PATKTDPSKF TAKKSKAVAK QGRAKYQFEI
MLQLGIPREE VSKFADPFYW VEYFPPLCQR DCNSFGARID WRRSFVTTNA NPYYDSFIRW
NMNRLREAGK IKFGKRYTIF SAKDNQPCMD HDRQVGEAVN PQEYTAIKIK VTEWPEAAQK
VLSEQSFDLN GKSVYLIAAT LRPETMYGQT CCFVSPKIEY GIFDAGNNDY YICTERAFKN
MSFQDLTPVR GYYQASAKIS GSVIIGAKIK APLSVYPELR VLPMETVLAN KGTGVVTSVP
SNSPDDYITA IDLQNKPEYY KIEREWASFE PVAIIETPTY GTVTAKTIIE QLKVKSPKDK
DALAQAKELA YKEDFYQGVM VIGKYKGEKV EDAKPKVKAD LIASNEAFVY DEPEGLVISR
SGDECVVSLQ DQWYTDYGED SWRAKAEQCL SQMNTYSPET KHGFEKVLGW LKNWALSRSY
GLGTKIPWDP QYLVESLSDS TIYMAYYTIS HFLHSDFYGR EKGLLDIKVE EMTDEVWDFV
FTNPTDDMSN LNTTISKDKL MKMRHEFQYF YPLDVRVSGK DLIPNHLTFF IYVHTAIFPE
EFWPRGIRAN GHLMLNNEKM SKSTGNFMTL EEIVKKFGAD AARIALADAG DTFEDANFDE
SNANAAILRL YNLKEWMEEV IKNDSELRTG SADEYNFFDL AFANEMNELI AATKDNYENA
WYKGALKSGL FDFQSARDYY RESTTSVGTG MHKELVRRYI EVQALLLTPI APHFAEYVWR
DILGKNESVQ YAHFPKVDSP INKSISDALA YVRNLSRSAR ETEGALLKKK KKGNDFDPKK
PSKLSLYISL AFPKWQDEYI EVVRDAFENL SLDFTPDFKQ KIAKIGDVKR GMQFVNTLKT
KLTVEKLPPN TVFNRKLTFS EVDTVKTTVT LLKKSPQATK IEEIQLIAID ENDNTKGKDI
ISGEEVEVPS VKQVQEAVPG QPAIVIANI
//
