ID A0A178EI45_9PLEO Unreviewed; 1008 AA.
AC A0A178EI45;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-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=IQ07DRAFT_529061 {ECO:0000313|EMBL:OAL55484.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL55484.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL55484.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL55484.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
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};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR EMBL; KV441637; OAL55484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EI45; -.
DR STRING; 765867.A0A178EI45; -.
DR InParanoid; A0A178EI45; -.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000077535; 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; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
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; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 3.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535}.
FT DOMAIN 69..252
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 268..461
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 477..641
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 668..718
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 795..926
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1008 AA; 113778 MW; 335BF8ECBF288A9F CRC64;
MHGLSLLRLG WRRPLRCPPV APSCARPRVS LQWASSLTDR KRRAEETGIE TLTAKWQPHW
DNLAPQWHSL RLSDKGNAYV LPMFPYPSGT LHLGHLRVYT ISDVLARFKH MQGYKVLHPI
GWDAFGLPAE NAAIERGVHP EKWTLQNIEA MKAQIKEMGG RWDWDSELRT CDPAFYKHTQ
SIFLMLHERG LAYQAESLVN YDPVDKTVLA NEQVDANGCS WRSGAKVEKK MLKQWFLKIK
AFQEPLLKDL DTLAEDGRWP EKVLAMQRNW IGRSEGSQLS FDVKSNDTSF RFNPIEVFTT
RADTLFGVQY LALSLSHPIV QRLAVNNDAL RAFLERAKDM PQDTKEGFLL SDISAENPIA
EITDASDSSI PIYVAPYVLD EYGSGAVMGV PGHDTRDHAF WRKNAGDSLI KVVIFPTQNS
TLAAMEPGHE DKPYTERGFV AADIATFGNL TSKQAMRKVV AAVRSTGKDA KMTSTWRLRD
WLISRQRYWG APIPIIHCGA CGPVPVPRDQ LPVELPSLPD SFFKDRTGNP LVEDESWKKT
TCPKCGSVAE RETDTMDTFM DSSWYFFRFL DSENEKELVD PKKAKDGLPV DLYIGGVEHA
ILHLLYARFI SKFLATTQVW PEGKRFLGEP FKRLITQGMV HGETFTDPET GRFLRPDEVD
ASNPTQPKII KTGVTAQVSY EKMSKSKYNG VDPGTTIAKY GADATRAHML FQAPVGDVLD
WDEKKIAGVQ RWLHRVVRLS RAVWLPDEKL DDFKITTKID SQLGDILEDL SGRRILRPYQ
PFVEKMIESL SDDDAKLWIK TQQTITSVVE SYSRTYSMNT IVSDLMILTN SIWDTPNSSA
ITPYLKWYST MHLIRMVAPI APGVGEEGWH SLMNLAAPAS KQSDLSTVFA SGFPTADLAI
LDQLTHKHKC VVQIDGKRRF QVTIPKLPKT ISPNDTEAVS KFILDELIQT EEGGKWLDKQ
TGMIWKKSLT GQPHPVYKIV PDDWNVIAVK EGALCNFVSP KTKRSSNV
//
