ID   SYL_CROS5               Reviewed;         853 AA.
AC   B1WSK6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   OrderedLocusNames=cce_4237;
OS   Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS   ATCC 51142)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX   NCBI_TaxID=43989;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51142 / BH68;
RX   PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA   Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA   Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA   Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT   "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT   important in the marine nitrogen cycle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
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; CP000806; ACB53585.1; -; Genomic_DNA.
DR   RefSeq; WP_009543691.1; NC_010546.1.
DR   AlphaFoldDB; B1WSK6; -.
DR   SMR; B1WSK6; -.
DR   STRING; 43989.cce_4237; -.
DR   KEGG; cyt:cce_4237; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001203; Chromosome circular.
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; 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; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..853
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091311"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           615..619
FT                   /note="'KMSKS' region"
FT   BINDING         618
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   853 AA;  97000 MW;  0D93907DD31424C4 CRC64;
     MESQYNAAEI EQKWQQDWVN QGLDKTPENS DKPKFYALSM FPYPSGNLHM GHVRNYVITD
     VIARLKRLQG YRVLHPMGWD AFGLPAENAA IDRNIPPADW TYKNIAQMKQ QLQTLGLSID
     WDREVATCSP DYYKWTQWLF LQFYQAGLAY QKEAAVNWDP IDQTVLANEQ VDSEGYSWRS
     GAKVERKLLR QWFFKITDYA EQLLTDLDKL TGWPDRVKLM QENWIGKSVG AYLEFPVKGS
     EEKIAVFTTR PDTVYGVTYV VLAPEHPLTP KVTTEGQKEA VEAFIEEVSN ESEIERTAED
     KPKRGILTGG TAVNPFNGEE IPILIADYVL YEYGTGAVMG VPAHDTRDFK FATEKELPIK
     VVIVPENSED NNPTLTEAYT EPGIMVNSGE FNGMQSTEGK TAIINYAEKQ GYGKARIQYR
     LRDWLISRQR YWGCPIPVVH CPSCGTVAVP DADLPVKLPE NVEFTGRGAS PLAKMEDWIN
     VPCPSCGEPA KRETDTMDTF IDSSWYYLRY TDAMNDQEAF KLEKANDWMN VDQYVGGIEH
     AILHLLYSRF FTKVLRDRGL VNVDEPFKRL LTQGMVQAMA YKNPKTGKYI PVDKVNPESP
     KDPDTGDDLE VFYEKMSKSK YNGVDPQKVL GKYGADTARM FILFKAPPEK DLEWDDADVE
     GQFRFLNRVW RLVNGYEKKQ GEVISNKELS KEEKDLRRAI HTAIKEISED LEGDYQFNTA
     VSELMKLSNA LNDAKCINSE VYQEGIETLL ILLAPFAPHI AEELWHNLGH ETSIHLETWP
     QVDPDALVVD EITLVIQIMG KTRGTIQVPA NSSKEELEKL ARESDIGQRN LDGKEVKKVI
     VVPGKLVNFV VPK
//