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
//
