ID A0A0D2GWB0_9EURO Unreviewed; 1124 AA.
AC A0A0D2GWB0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=Z517_09088 {ECO:0000313|EMBL:KIW76644.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW76644.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW76644.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW76644.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) 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; KN846974; KIW76644.1; -; Genomic_DNA.
DR RefSeq; XP_013280452.1; XM_013424998.1.
DR AlphaFoldDB; A0A0D2GWB0; -.
DR STRING; 1442368.A0A0D2GWB0; -.
DR GeneID; 25308578; -.
DR VEuPathDB; FungiDB:Z517_09088; -.
DR HOGENOM; CLU_004174_1_1_1; -.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000053029; 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 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:KIW76644.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000053029}.
FT DOMAIN 65..131
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 215..805
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 843..968
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 144..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1124 AA; 127054 MW; DF0B9559354826D4 CRC64;
MATQIPVDPT LTSANTLKLE NTHNRDVLIA IEKKYQKQWQ ESKIFESDAP TTTEIPFDSV
PAAEIREKYP KYFGTFAYPY MNGSLHAGHS FTVSKVEFTA GFNRLTGKRV LFPLGFHCTG
MPIKACADKL VEDVKKFGQN FENYHEDEDE PAPDTNGAPI APTQGVNVKD DLTKFKSKKG
KQAAKTVKAN YQFQTMLAMG IPKEEIHKFA DANYWLEYFP PICQQDLIDF GARIDWRRKF
VTTDANPYYD AFVRWQMNRL HELNKILYGK RYTIYSPKDG QPCMDHDRTK GEGVGPTEYT
ALKLRVKEWS PDAAKAVESK IPQDASVYFV PATLRPETMY GQVCCFVGPK IKYGIFKVSE
KEYYVVTKRA AWNMAFQGTF FDQEHFPRNQ DELQPVVELP GSAFVGTLVN APLSVHKEGV
RILPMETVSA TKGTGVVTSV PSDSPDDFAT VKELAKKADF YGIQKEWAEL EIIPIIDTPA
YGNLAAKFLV ETKKIQSPKD TTLLAEAKDL AYKEGFYNGT MLVGEFKGQK VSDAKDKVRS
ALIASGEAFP FADPSAEVIS RSGDECVVAY VPQWFLNYGE NDKEWQQTVL DYVKDKNGLE
TYAQETENQF VANLEWLNQW ACARTYGLGS KLPWDPSFLV ESLSDSTIYM SYYTVAHFLH
GDKFGKEPGL LDIKAEQMTD DVWDYIFTRT SDVKKVSDST RISVADLQTM RRSFEYWYPL
DLRSSGKDLI PNHLTFFLYI HLALFPREYW PKSVRSNGHL LLNGEKMSKS TGNFLTLSQA
VKKFGADATR IALADAGDGM EDANFEEKSA NAAIMRMYIL KDWIEDTLKD EGLRKTQGEV
IWDKLFEDEM NLLVHEAYKH YSETNYKLAL KSALYDFQSA RDFYRDACVS GGIPLSRPLV
VRFAELQCLL ISTIAPHWAE YIWLEVLHKD QSIQLARWPT DVPEADPSLT ATRDYVKATS
SNITSAEAQA AKKMAKGKAV AFDPRKPKQI TIFVASRFPA WQDKYVDLVR TLLENASLDD
DKALNASVAK MGKGPEMKKA MPFVQGLKRR LVVNKESPEA VFERKLPFDE VHILTEMKKG
LMKNTGCKDV KVVSVTDENR QSLPSMAELA VPGQPSFLFE NVDA
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