ID A0A135LW58_PENPA Unreviewed; 1125 AA.
AC A0A135LW58;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=PGRI_002010 {ECO:0000313|EMBL:KXG53151.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG53151.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG53151.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG53151.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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 -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363039}.
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:KXG53151.1}.
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DR EMBL; LHQR01000014; KXG53151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LW58; -.
DR STRING; 5078.A0A135LW58; -.
DR OMA; KFIEWQF; -.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000070168; 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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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 Pfam; PF09334; tRNA-synt_1g; 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363039};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363039};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363039};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168}.
FT DOMAIN 68..139
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 704..804
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 839..950
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1125 AA; 126336 MW; 1C2A99780696BE50 CRC64;
MAAAAASVAE LDPSNSSKNT LKLENTEKRD SLIAIEKKYQ AQWKENKVFE VDAPSFEEAP
QGALTPAELR EKYPKFFGTM AYPYMNGTLH AGHSFTASKV EFMAGFARME GKRALFPLGF
HCTGMPIKAC ADKLANEVKK FGQGFEGYSE EAEAAEDLRA APTQEVKAEA SEKFSGKKSK
AAAKTVKMKY QFQIMLAIGV PLEEIHKFAD AAHWLDHFPP LAIRDLDSMG ARVDWRRQFV
TTDANPYYDA FVRWQMNRLH ELGKIMYGNR YTVYSPKDGQ PCMDHDRTEG EGIGPQEYSA
LKLQVKEWSP KMAELVKGKI EDDAKVYFVP ATLRPETMYG QTCCFVGPKI NYGLFKLKEK
EYIVVTKRAA WNMAFQGHFF GDKFPKTQDE LPQVLEVQGS AFVGTLVNAP LSFHTEGVRI
LPMDSVSASK GTGVVTSVPS DSPDDYATLM DLAKKAEYYG IQKEWAELEI FPLIDTPTYG
NLTAPALVKE LKINSPKDAT QLAQAKDLAY MEAFYKGTML VGNYKGEPVS DAKEKVRKDL
YESGDAFPFA DPMGKVVSRS GDDCVVAYLG QWFLNYGEND AEWQQETLNH VVNNLNTYSA
ECKNGFEKNL SWLNRWACAR TYGLGSKLPW DKQFLVESLS DSTVYMAYYT IAHLLHGDRY
GKTTGPLKVT AEQMTDEVWD YIFTRREISD ELIASSGISK ESLQQMRREF EYWYPLDVRV
SGKDLIQNHL TFFLYIHIAL FPKEYWPRGV RANGHLLLNG EKMSKSTGNF LTLKDAVDKF
GADATRIAFA DAGDSIEDAN FEESVANSNI LRLYTLKEWI EEIAKDETLR TGPADAFADK
LFNNELNSLV RETQKHYQDT NFKLALKSGL YDFTSSRDSY REASTAAGVG MHRDTILRYI
ELQALMLAPI TPHWAEHIWL EVLKKSESIH FAQFPAVPEP SPELTAAQNY VRGTASNIMS
SEANYAKKLS KGKNISFDPR KPKKLTIFVA KKFPTWQEKY IDLVRDSFDS LSLSFNDKEL
SAKVGKLGEM KKAMPFVQSL KRRLVNAGES PATVFDRKLP FDEFAVISEM VGGLKRTSGF
KEIEVIAVDE GGKTGEVVGT GEKREGLSGE NAVPGTPTFQ FVNVE
//
