SYL_SYNSC
ID SYL_SYNSC Reviewed; 875 AA.
AC Q3AJU8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=Syncc9605_1380;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-2005) 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: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; CP000110; ABB35134.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3AJU8; -.
DR SMR; Q3AJU8; -.
DR STRING; 110662.Syncc9605_1380; -.
DR EnsemblBacteria; ABB35134; ABB35134; Syncc9605_1380.
DR KEGG; syd:Syncc9605_1380; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_3; -.
DR OMA; TFMVLAP; -.
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 Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR43740; PTHR43740; 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; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 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..875
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334829"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 60..70
FT /note="'HIGH' region"
FT MOTIF 634..638
FT /note="'KMSKS' region"
FT BINDING 637
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 875 AA; 96528 MW; AC3754A1958463C4 CRC64;
MPSAGSVNAA NPAVDTSAQT GRYDPTALEQ RWQESWKADG VDTTEVGGEK PGFFALSMFP
YPSGSLHMGH VRNYVITDVI ARVQRMLGHA VLHPMGWDAF GLPAENAAIE RNVDPGEWTD
RNIDQMRAQL DRLGLSIDWS REQATCHSDY YRWTQWLFLE LLEGGLAYRK NATVNWDPVD
QTVLANEQVD GDGRSWRSGA LVEQRQLNQW FLRITDYAEP LLNDLDALKG WPERVRTMQA
NWIGRSEGAE ISFNVEGAQN QTITVFTTRP DTLAGASYVV LAPENELVDS LSSEEQKDTV
EAFRKEVARL STIERTCDDR PKRGVPIGSH VINPLTGVVL PVWIADYVLA EYGTGAVMGV
PAHDQRDIAF AQSNGLPIQQ VIDAEGAAEA IAAGQAWTDA GTLVNSGSFD GTASSEAKGA
ITGHGAEQGW ARSKVTYRLR DWLISRQRYW GCPIPVIHCD NCGAVPVPRE DLPVELPRGI
DLSGKGGSPL SQQSDWVNVA CPRCGKPAKR ETDTMDTFMC SSWYFLRFAD PHNTEKPFSK
EAVNRWLPVK QYVGGIEHAI LHLLYARFFT KALKDRGLID INEPFERLLT QGMVQGVTYR
NATTGKYIAP ADVADAEDPR DPNTGDKLEV LFEKMSKSKY NGVDPAAVID RYGADTARMF
ILFKAPPEKD LEWDDADVEG QFRFLQRLWR LVEAGSARID SLEPMQRPAD LSDADSDVRR
ALHLAIEAVS EDLSDEIQLN TAISELMKLS NAISSTGIDA LSAPVLQEAL SGLVRLLAPF
APHLAEEFWN RLGGSGSVHR QSWPVLDPTA LVQDSVEVVI QVKGKVRGKL QVPASAGKEE
LERLALASDV AEKWLEGAAP RRVIVVPGKL VNLVP