ID A0A0R3DFQ8_9BRAD Unreviewed; 874 AA.
AC A0A0R3DFQ8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=AOQ71_24055 {ECO:0000313|EMBL:KRQ07197.1};
OS Bradyrhizobium manausense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=989370 {ECO:0000313|EMBL:KRQ07197.1, ECO:0000313|Proteomes:UP000051936};
RN [1] {ECO:0000313|EMBL:KRQ07197.1, ECO:0000313|Proteomes:UP000051936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR3351 {ECO:0000313|EMBL:KRQ07197.1,
RC ECO:0000313|Proteomes:UP000051936};
RA De Araujo J.L., Zilli J.E.;
RT "Draft Genome Sequence of Bradyrhizobium manausense Strain BR 3351T, a
RT Novel Symbiotic Nitrogen-Fixing Alphaproteobacterium Isolated from
RT Brazilian Amazon Rain Forest.";
RL Submitted (SEP-2015) 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:KRQ07197.1}.
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DR EMBL; LJYG01000099; KRQ07197.1; -; Genomic_DNA.
DR RefSeq; WP_057751961.1; NZ_LJYG01000099.1.
DR AlphaFoldDB; A0A0R3DFQ8; -.
DR STRING; 989370.AOQ71_24055; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000051936; 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 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 38..172
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 222..413
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 432..616
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 629..669
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 715..833
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 630..634
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 874 AA; 97935 MW; 607DF0CA59229A1F CRC64;
MTSERYNARD AEPRWQRKWD EQAIFVSKND DSRPKYYVLE MFPYPSGRIH IGHVRNYTLG
DVLARFMRAK GFNVLHPMGW DAFGLPAENA AIERKVAPKA WTYDNIAAMK KQLRSIGLSL
DWSREFATCD PSYYKHQQKM FLDMLAAGLA EREKRKLNWD PVDMTVLANE QVIDGRGWRS
GAIVEQREMS QWVFKITKYA QELLSALDSL DRWPDKVRLM QRNWIGRSEG LLIRFALDQA
TTPAGESELK IFTTRPDTLF GAKFMAISAD HPLAQAAAAK NPDLAEFISD IKKIGTAQSI
IDTAEKQGFD TGIRAVHPFD PDWKLPVYVA NFVLMEYGTG AIFGCPAHDQ RDLDFVNKYA
LGNTPVVCPE GQDPKSFVIT DTAYDGDGRM INSRFLDGMT IEQAKEEVAK RLESEMRGNA
PVAERQVNFR LRDWGISRQR YWGCPIPVIH CPRCDVVPVP DDQLPVVLPE DVSFDKPGNA
LDHHPTWKHV TCPKCGGSAS RETDTMDTFV DSSWYFARFT DPWNEKAPTT PAIANRMLPV
DQYIGGVEHA ILHLLYSRFF TRAMKATGHL ALDEPFAGMF TQGMVVHETY QKADGSWVQP
AEVKIEVGGN GRRAILLATG EDVTIGPIEK MSKSKKNTVD PDDIIATYGA DVARWFMLSD
SPPDRDVIWS DERVQGASRF VQRLWRLVND AVEVSKTAPA TRPGSFSDDA TALRKAAHGA
LDKVTSGVER LHFNVCLAHI REFTNSFSEV LQRPGQPAPD LAWAIREASQ ILVQLFSPMM
PHLAEECWQV LGQPGLVSEA SWPQIERDLL VEDSVTLVVQ VNGKKRGEVT VATVAQNPEI
EAAALALDAV KLALDGKPVR KVIIVPKRIV NVVG
//
