ID   SYL_CYAP4               Reviewed;         858 AA.
AC   B8HM05;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
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=Cyan7425_3031;
OS   Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC   Cyanothece.
OX   NCBI_TaxID=395961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7425 / ATCC 29141;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP001344; ACL45365.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8HM05; -.
DR   SMR; B8HM05; -.
DR   STRING; 395961.Cyan7425_3031; -.
DR   KEGG; cyn:Cyan7425_3031; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
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.
FT   CHAIN           1..858
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199190"
FT   REGION          584..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           619..623
FT                   /note="'KMSKS' region"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   858 AA;  97261 MW;  0DAA53022B113E82 CRC64;
     MESRYQPTAI EEKWQQTWAE VGIDQTPTDR SKPKFYALSM FPYPSGNLHM GHVRNYTITD
     VIARVRRMQG YRVLHPMGWD AFGLPAENAA IKRGIHPAKW TADNITQMRS ELKRLGLSYD
     WNCELATCSP DYYRWTQWIF LQFYQAGLAY QKEAAVNWDP IDQTVLANEQ VDSEGRSWRS
     GAKVERKLLR QWFLKITDYA EELLQDLDQL TGWPEKVRKL QANWIGKSTG AYLEFPIVGR
     DEKISVYTTR PDTVYGVSYV VLAPEHPLTL QVTTKKQLKA VKSFIQEVTA ASEIERTAED
     QPKRGIATGG KAINPFTGAE IPIWIADYVL YEYGTGAVMG VPAHDSRDFK FAQTYQLPIR
     QVIIPPDPDL NEQPILQEAY TEPGLLINSG EFDGMPSTDA KAAIVAKAEA TGWGQARVQY
     RLRDWLISRQ RYWGAPIPVI HCPQCGIVPV PEADLPVVLP DDVQFSGRGP SPLAQLESWV
     KVNCPTCNTP ARRETDTMDT FIDSSWYYLR YPDAQNDQQV FDPAKTNDWL PVDQYVGGIE
     HAILHLLYSR FFTKVLRDRG LLNFDEPFQR LLTQGMVQGL TYTNPNRSDS SRYIPSNLVD
     PNDPKDPETG EPLEVSYQTM SKSKYNGVAP EEVINKYGAD TARMFILFKA PPEKDLEWDD
     ADVEGQFRFL NRVWRLVTQY PVIEPTTKQG DALAKEEKEL RRAIHTAIKE ITADLGEEYQ
     LNTAVSELMK LSNALTDASC KDSVIYTEGI ETLLLLLAPF APHISEELWQ QLGHTTSVHQ
     QSWPQVDPSA LIVDEITIVI QILGKTRGTI QVPASSSREE LEEYARQTPV AQRYLEGKTI
     KKVIVVPGKL VNFVVADA
//