ID A0A2T9ZF52_9FUNG Unreviewed; 972 AA.
AC A0A2T9ZF52;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=BB560_002300 {ECO:0000313|EMBL:PVV03233.1};
OS Smittium megazygosporum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133381 {ECO:0000313|EMBL:PVV03233.1, ECO:0000313|Proteomes:UP000245609};
RN [1] {ECO:0000313|EMBL:PVV03233.1, ECO:0000313|Proteomes:UP000245609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-DP-2 {ECO:0000313|EMBL:PVV03233.1,
RC ECO:0000313|Proteomes:UP000245609};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
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}.
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:PVV03233.1}.
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DR EMBL; MBFS01000260; PVV03233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9ZF52; -.
DR STRING; 133381.A0A2T9ZF52; -.
DR Proteomes; UP000245609; 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 HAMAP; MF_00049_B; Leu_tRNA_synth_B; 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; 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; 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; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 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:UP000245609}.
FT DOMAIN 116..253
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 302..487
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 502..624
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 706..739
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 793..918
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 972 AA; 111153 MW; B38BFFE9CC70C35F CRC64;
MLFSVIQHSN LAQPSFYCRH NFKLLSLAYS KNQIFKGTKS PQNHFHFTKR LATTVSQPPS
TSINEDLINH SENEKKWSKR WGDSSRKTSL EILQKLSHNS TKLPALSEES IDRHFYVLAM
FPYPSGKLHM GHVRVYTISD AIARHSNITF TTVTHPMGWD AFGLPAENAA IDRGLNPALW
TKENIDNMRT TLKSMLLDID WDKEFATCDP EFYRWTQFLF LQLWKRGLVY QKEAEVNWDP
IDKTVLANEQ VDKNGCSWRS GAKIEKRKLK QWFIRISKFS ESLLQNLDLL ENWPEKVKQM
QRNWIGKSIG AEFTFSTEIN GSEFKIPVFT SRPDTIFGVS YIAISKNHQL ASERNFSKEK
AEEIKEFIKK IDSFKGINET NSKLGIDTGL FAKHPLDPNR KIPIFIANYV LSDYGSGAVM
GVPAHDQRDY DFAISNSLNN FASVIESGSG EKVEIPFCDK GILIKNSQNG IFGGLSSEEA
SERILEKCIQ SGSGLKKTQY KLRDWLVSRQ RYWGTPIPFI HCADCGPVPV PDSDLPVKLP
LDIQLSQRGG NVLDTLDDWK KVECPSCGKQ AKRETDTMDT FVDSSWYYFR FLDHKNNNLP
FDPQIIQKDM PVDIYIGGIE HSILHLLYSR FLTKSIQTDG KFKFYSSKND AQAEHEHFQT
LEQSSLGKSE PFLSLLTQDP KTERFLHPSE LEFTSGSNET PIVTYEKMSK SKHNGVDPES
VISQYGADVT RLYMLFKAPP QDVLEYDTKS IVGIHRWVLK LTRIINTIKP KFKPIKDMKE
LADREDWSKE NNEIYKLTQT SIKMATEVFE KNYSFNTVIA SLMTLSNNIS STLETRNLDE
LHPSVIYAMD CLLIILSPMA PSVSEELFER LHATDKEYKG SIFAYKWPKV DETGFLSEMK
TCVVQVNGKT KMTLEVETEL FNDKSLLLDK LSSHSEVKAV LLNKKTGTPL DIIKTIVVPR
RSLVNYVVSK NK
//
