GenomeNet

Database: UniProt
Entry: A0A3N1AXP1_9ACTN
LinkDB: A0A3N1AXP1_9ACTN
Original site: A0A3N1AXP1_9ACTN 
ID   A0A3N1AXP1_9ACTN        Unreviewed;       964 AA.
AC   A0A3N1AXP1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=EDC02_3213 {ECO:0000313|EMBL:ROO61281.1};
OS   Micromonospora sp. Llam0.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=2485143 {ECO:0000313|EMBL:ROO61281.1, ECO:0000313|Proteomes:UP000275308};
RN   [1] {ECO:0000313|EMBL:ROO61281.1, ECO:0000313|Proteomes:UP000275308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Llam0 {ECO:0000313|EMBL:ROO61281.1,
RC   ECO:0000313|Proteomes:UP000275308};
RA   D'Agostino P.;
RT   "Genome mining of underrepresented organisms for secondary metabolites.";
RL   Submitted (NOV-2018) 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:RU363039}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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:ROO61281.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; RJJY01000001; ROO61281.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1AXP1; -.
DR   Proteomes; UP000275308; 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   Gene3D; 3.40.50.620; HUPs; 3.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000275308}.
FT   DOMAIN          84..186
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          312..506
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          814..929
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           739..743
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         742
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   964 AA;  107332 MW;  7F104ABD1E6EF696 CRC64;
     MPTTDTHSPQ PTLRWRPTMS EAVETAADTP PFRYTAAMAG EIERQWQQRW ERDGTFHAPN
     PVGPLADPAH PRADAEKLFL LDMFPYPSGA GLHVGHPLGF IGTDCYGRYQ RMAGRNVLHA
     MGFDAFGLPA EQYAVQTGQH PRTTTEANIE RYRAQLRMLG LAHDDRRSVA TTDVEFYRWT
     QWIFLQVFNS WYDTEAGKAR PVSELIAAYE SGRRATPDGR AWSELSDRER RELVDAHRLA
     YVSEAPVNWC PGLGTVLANE EVTADGRSER GNFPVFKRSL RQWMMRITTY ADRLLSDLDL
     LDWPEPIKLM QRNWIGRSTG AHITFPTGAA PIEVFTTRPD TVFGATYMVL APEHALVDDL
     VPTAWPAGTR PAWTGGHATP AEAVEAYRKQ AAGRTDAERQ AETRDKSGVF VGAYATNPVN
     GARLPIFIAD YVLAGYGTGA IMAVPAQDER DWDFAEVFDL PIVRTVTPPE DFTGKAYTGD
     GPAMNSDFLN GLGVTEAKER IIAWLEAGGH GRGAVTYRLR DWLFSRQRYW GEPFPIVYDT
     TGLPIPLPEE MLPLELPEID DFSPRTFDPD DAASDPETPL SRAADWVEVE LDLTGVPGAP
     AGRQRYRRET NTMPQWAGSC WYELRYADPA NSDAFVDPAN ERYWMGPAST TDCGGVDLYV
     GGVEHAVLHL LYARFWHKVL FDLGHVSSVE PFRRLFNQGY IQAYAYTDAR GAYVDAAAVT
     ERDGGWFHGD VAVDREYGKM GKSLRNVVTP DEMCEAYGAD TFRVYEMSMG PLEVSRPWET
     RAVVGSYRFL QRVWRALVDE RTGASRVTDD PADDELRRLT HRVIDGVRSD MDGLRFNTAI
     AKLIELTNAL TRLPATPREV AEPLVLMLAP FAPHVAEELW QRLGHTGSLT YVDFPVADPA
     LLRAASVTYP VQVAGKVRGR VEVPAEAAED EVRAAALAAV AEHLAGRTPR KVIVVPGRMV
     SVVP
//
DBGET integrated database retrieval system