ID A0A0N0E2N9_9PSED Unreviewed; 868 AA.
AC A0A0N0E2N9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN ORFNames=PF66_04285 {ECO:0000313|EMBL:KPA89132.1};
OS Pseudomonas fuscovaginae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA89132.1, ECO:0000313|Proteomes:UP000037931};
RN [1] {ECO:0000313|EMBL:KPA89132.1, ECO:0000313|Proteomes:UP000037931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA89132.1,
RC ECO:0000313|Proteomes:UP000037931};
RX PubMed=26422147;
RA Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S., Mauleon R.,
RA Cruz C.V., Oliva R.;
RT "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor
RT Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot.";
RL PLoS ONE 10:E0139256-E0139256(2015).
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, ECO:0000256|HAMAP-
CC Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC 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:KPA89132.1}.
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DR EMBL; JSYZ01000017; KPA89132.1; -; Genomic_DNA.
DR RefSeq; WP_054063737.1; NZ_JSYZ01000017.1.
DR AlphaFoldDB; A0A0N0E2N9; -.
DR STRING; 50340.PF66_04285; -.
DR PATRIC; fig|50340.43.peg.1589; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000037931; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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-RELATED; 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|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00049}.
FT DOMAIN 39..171
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..407
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 423..579
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 623..660
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 708..831
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 627..631
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 630
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 868 AA; 97164 MW; BAA4C0391459A0E9 CRC64;
MHEHYQPREI ENAAQSFWDE QKSFEVSEQP GKDTYYCLSM FPYPSGKLHM GHVRNYTIGD
VIARYQRMQG KNVLQPMGWD AFGMPAENAA MKNKVAPAKW TYENIAYMKS QLRSLGLAVD
WSREVTTCKP DYYRWEQWLF TRLFEKGVIY RKNGTVNWDP VDQTVLANEQ VIDGRGWRSG
ALIEKREIPM YYFKITAYAD ELLESLDELP GWPEQVKTMQ RNWIGKSRGM EVQFPYDVDS
IGEAGTLKVF TTRPDTLMGA TYVAVAAEHP LATQAARNNP ELQAFIAECK AGSVAEADVA
TQEKKGLPTG LFVAHPLTGE KLPVWVANYV LMHYGDGAVM AVPAHDERDF EFASKYHLPI
KSVVRTSSGD THPAPWQDAY GEHGTLINSG EFDGLDFAGA FDAIEAALIR KNLGASRTQF
RLRDWGISRQ RYWGCPIPII HCDSCGDVPV PEDQLPVVLP EDVVPDGAGS PLARMPEFYE
CNCPKCGQPA KRETDTMDTF VESSWYYARY ASPRYEGGLV DPKAANHWLP VDQYIGGIEH
AILHLLYARF FHKLMRDEGL VSSNEPFKNL LTQGMVVAET YYRREANGGY TWYNPADVEL
ERDSKAKIIG ARLISDGLPV EIGGTEKMAK SKNNGVDPQS MIEQYGADTC RLFMMFASPP
DMSLEWSDSG VEGAHRFLKR VWRLAQAHVT QGLPGKLDLT ALNDEQKAVR RSIHLAIKQA
SQDVGQNHKF NTAIAQVMTL MNVLEKTPQG STQDRALIQE GLETVALLLA PITPHISHEL
WKQLGQDGAI IDAGWPVLDE SALVQDSLVL VIQVNGKLRG QIEMPASATR EEIEAAARVN
ENVLRFIDGL TIRKVIVVPG KLVNIVAS
//