ID S2EXA1_9PSED Unreviewed; 868 AA.
AC S2EXA1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=PG5_39410 {ECO:0000313|EMBL:EPA95731.1};
OS Pseudomonas sp. G5(2012).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1268068 {ECO:0000313|EMBL:EPA95731.1, ECO:0000313|Proteomes:UP000014290};
RN [1] {ECO:0000313|EMBL:EPA95731.1, ECO:0000313|Proteomes:UP000014290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G5(2012) {ECO:0000313|Proteomes:UP000014290};
RA Park S., Lee J.-H., Cho Y.-J., Chun J., Hur H.-G.;
RT "Draft Genome Sequence of Pseudomonas sp. Strain G5, Isolated from a
RT Traditional Indigo Fermentation Dye Vat.";
RL Submitted (MAR-2013) 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, 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:EPA95731.1}.
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DR EMBL; APIO01000059; EPA95731.1; -; Genomic_DNA.
DR RefSeq; WP_020798746.1; NZ_APIO01000059.1.
DR AlphaFoldDB; S2EXA1; -.
DR GeneID; 72197394; -.
DR PATRIC; fig|1268068.3.peg.3771; -.
DR eggNOG; COG0495; Bacteria.
DR Proteomes; UP000014290; 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; 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..405
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 615..659
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 707..832
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; 97021 MW; 924AA82C324BAF40 CRC64;
MHEQYQPREI EAAAQSFWDE QKSFEVSEQP GKETYYCLSM FPYPSGKLHM GHVRNYTIGD
VISRYQRMQG KNVLQPMGWD AFGMPAENAA MKNNVAPAKW TYENIAYMKS QLRSLGLAVD
WSREVTTCKP DYYRWEQWLF TRLFEKGVIY KKSGTVNWDP VDQTVLANEQ VIDGRGWRSG
ALIEKREIPM YYFKITAYAD ELLESLDELT GWPEQVKTMQ RNWIGKSRGM EVQFPYNVDS
IGEAGTLKVF TTRPDTLMGA TYVAVAAEHH LATLAAQNNP ELQAFIAECK GGSVAEADVA
TQEKKGLPTG LFVEHPLTGE KLPVWVANYV LMHYGDGAVM AVPAHDERDF EFAHKYNLPV
KSVVRTSAGD TNPAPWQDAY GEHGTLINSG EFDGLDFVGA FDAIEVALIK KELGASRTQF
RLRDWGISRQ RYWGCPIPII HCTTCGDVPV PEDQLPVVLP EDVVPDGAGS PLARMPEFYE
CSCPKCGQPA KRETDTMDTF VESSWYYARY ASPHFEGGLV EKSAADHWLP VDQYIGGIEH
AILHLLYARF FHKLMRDEGL VSSNEPFKNL LTQGMVIAET YYRREANGAY TWFNPADVEL
ERDSKAKVIS AKLIADGLPV EIGGTEKMAK SKNNGVDPQS MIDQFGADTC RLFMMFASPP
DMSAEWSDSG VEGSHRFLKR VWRLAQAHVT QGLPGQLDVA GLNDEQKAIR RSIHQAIKQA
SHDVGQNHKF NTAIAQVMTL MNVLEKAAQG TEQDRALVQE GLETVTLLLA PITPHICHEL
WHRLGHADPV IDAGWPVLDE SALVQDSLTL VIQVNGKLRG QIEMPASATR EEVEAAARAN
ENVLRFVDGL TIRKVIVVPG KLVNIVAS
//
