ID   SYL2_RHIJ3              Reviewed;         876 AA.
AC   Q1MA25;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Leucine--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00049};
DE            Short=LeuRS 2 {ECO:0000255|HAMAP-Rule:MF_00049};
GN   Name=leuS2 {ECO:0000255|HAMAP-Rule:MF_00049};
GN   OrderedLocusNames=RL4732;
OS   Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841) (Rhizobium
OS   leguminosarum bv. viciae).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium;
OC   Rhizobium johnstonii.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 114642 / LMG 32736 / 3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
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:0000255|HAMAP-Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR   EMBL; AM236080; CAK10215.1; -; Genomic_DNA.
DR   RefSeq; WP_011654061.1; NC_008380.1.
DR   AlphaFoldDB; Q1MA25; -.
DR   SMR; Q1MA25; -.
DR   EnsemblBacteria; CAK10215; CAK10215; RL4732.
DR   KEGG; rle:RL4732; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   Proteomes; UP000006575; Chromosome.
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; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..876
FT                   /note="Leucine--tRNA ligase 2"
FT                   /id="PRO_0000334803"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           632..636
FT                   /note="'KMSKS' region"
FT   BINDING         635
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   876 AA;  97967 MW;  65A2A38FF62B870A CRC64;
     MATERYNPRD AEPRWQQKWN EDKVFETDNA DPREKYYVLE MFPYPSGRIH MGHVRNYAMG
     DVVARYKRAR GYNVLHPMGW DAFGMPAENA AMERGVHPAS WTYQNIGSMK AQLKAMGLSL
     DWSREFATCD VEYYQHQQHL FLDFLEKGLV YRKQSKVNWD PVDNTVLANE QVIDGRGWRS
     GALVEQRELT QWFFKITDFS QDLLDALDTL DQWPEKVRLM QKNWIGRSEG LTIRWEIVPE
     TAPAGESEVT VYTTRPDTLF GASFLAIAAD HPLAKDAAAK NPEIEAFCDE CRRAGTSLAA
     LETAEKKGMD TGIRVRHPLD PSWELPVYIA NFVLMDYGTG AIFGCPSGDQ RDLDFARKYG
     LPVVAVVMPR DGDAASFSVG DTAYDGDGVM INSRFLDGKT TEEAFNIVAD RLSAASLGNA
     PQGERKVNFR LRDWGISRQR YWGCPIPVIH CDDCGVVPVP KADLPVKLPD DVTFDQPGNP
     LDRHPTWRHV SCPNCGKDAR RETDTMDTFV DSSWYFTRFT APWEDKPTDP EAANRWLPVD
     QYIGGIEHAI LHLLYSRFFT RAMRETGHVA ATEPFKGLFT QGMVVHETYS RGAGASREWV
     APADIRIDEL DGKRRAFLLT NNEEVSIGSI EKMSKSKKNV VDPDDIIASY GADTARFFVL
     SDSPPERDVI WSEAGVEGAH RFTQRLWRLI SEAADALSAV APAPATDGEA LSISQAAHKT
     LKAVQNDYDK LWFNKAVARI YELVNALAAP MTKVAAGEGD ATYRAAVRDA AEILIQLVSP
     MTPHLAEECW AALGNEGLLA RASWPQYDET LVIENSVVLP VQINGKKRAE LTISRDADQN
     TVTDAVLDLD AVKNALNGQA PKKIIVVPQR IVNIVV
//