GenomeNet

Database: UniProt
Entry: H5U4D3_9ACTN
LinkDB: H5U4D3_9ACTN
Original site: H5U4D3_9ACTN 
ID   H5U4D3_9ACTN            Unreviewed;       978 AA.
AC   H5U4D3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 68.
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   ECO:0000313|EMBL:GAB40591.1};
GN   ORFNames=GOSPT_111_00060 {ECO:0000313|EMBL:GAB40591.1};
OS   Gordonia sputi NBRC 100414.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1089453 {ECO:0000313|EMBL:GAB40591.1, ECO:0000313|Proteomes:UP000005845};
RN   [1] {ECO:0000313|EMBL:GAB40591.1, ECO:0000313|Proteomes:UP000005845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100414 {ECO:0000313|EMBL:GAB40591.1,
RC   ECO:0000313|Proteomes:UP000005845};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia sputi NBRC 100414.";
RL   Submitted (FEB-2012) 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:GAB40591.1}.
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; BAFC01000109; GAB40591.1; -; Genomic_DNA.
DR   RefSeq; WP_005207662.1; NZ_BAFC01000109.1.
DR   AlphaFoldDB; H5U4D3; -.
DR   eggNOG; COG0495; Bacteria.
DR   Proteomes; UP000005845; 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   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; 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; 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          82..189
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          312..518
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          825..942
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           749..753
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         752
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   978 AA;  108889 MW;  E6011E6946AE0C28 CRC64;
     MSTADISTSE GAADQASTDP ASATPGHRYT ARLAGEIEER WQREWTQRHA FEAPNPVGPL
     AGDMSAFDGS GPDAPDKLFV QDMFPYPSGA GLHVGHPLGF IASDVFARFQ RMSGANVLHT
     MGFDSFGLPA EQYAVQTGTH PRTTTEANIE RYLGQIRRLG LGHDERRRVA TTDVSFYRWT
     QWIFLQIYNA WYDDEAGKAR RVDELIAEFD SGARTLDDGR VWADLSAPEK SDLVDSYRLV
     YLSDSLVNWA PGLGTVLANE EVTADGRSDR GNFPVFRKHL RQWMMRITAY SDRLLDDLEV
     LDWPEKVKTM QRNWIGRSRG AQVQFPVPGV PAQADGEVTV DVFTTRPDTL FGATYVVLAP
     EHPLVDVLTA DTWPSGAEGA AVDERWTNGA STPAEAIKNY RASIAAKSDL ERQENKEKTG
     VFTGSFATNP VNGQQVPVFV ADYVLMGYGT GAIMAVPAHD SRDYEFATVF GLPIVEVIGS
     EAGISEEAYV GDGPLVNSGF LDGKNVDDAK TAIIEWLEEQ GSGQGTVQYK LRDWLFARQR
     YWGEPFPIVY DEEGRAHALP ESMLPVELPE VEDYAPVAFD PDDADSEPSP PLEKATDWIH
     VELDLGDGPK KYKRDANVMP QWAGSSWYQL RYIDPTNEEE FCAKENEAYW MGPRPELHGL
     SDPGGLDLYI GGVEHAVLHL LYSRFWHKVL FDLGYVTSSE PYRKLFNQGM IQAYAYTDSR
     GIYVPAEEVT EVDGEFVYNG EKVTQEYGKM GKSLKNSVTP DDIAAEYGAD TLRLYEMYMG
     PLDQSRPWAT KDVVGLQRFL QRAWRLVVDE ESGAVRVADI EPDDETLRLL HKTIAEVRED
     YNGLRDNIAV AALIKLTSHL TKQFPDGAPR STVEQLVLML APLAPHISEE LWSRLGHDEL
     LVRGPFPVAD ERYLVDDTVE IPIQVKGKVR SRITVPADAD EETIRAAALD DEKILAILDG
     QPPRKVIVVP GRMVNIVP
//
DBGET integrated database retrieval system