ID   SYL_TRIV2               Reviewed;         872 AA.
AC   Q3M3A3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
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}; OrderedLocusNames=Ava_4936;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA24533.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3M3A3; -.
DR   SMR; Q3M3A3; -.
DR   STRING; 240292.Ava_4936; -.
DR   EnsemblBacteria; ABA24533; ABA24533; Ava_4936.
DR   KEGG; ava:Ava_4936; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000002533; 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   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..872
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009289"
FT   MOTIF           42..52
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   872 AA;  98513 MW;  20AB279E2EC4045C CRC64;
     MDSRYNPAIL EEKWQKTWVE LGLDKTQTQS NKPKFYALSM FPYPSGSLHM GHVRNYTITD
     VIARLKRMQG YRVLHPMGWD AFGLPAENAA IDRGVPPANW TYQNITQMRQ QLQRLGLSID
     WDSEVATCSP DYYKWTQWIF LQFLQAGLAY QKEAAVNWDP IDQTVLANEQ VDNEGRSWRS
     GAIVERKLLR QWFLKITDYA EELLNDLDKL TGWPERVKLM QANWIGKSVG AYLEFPIVGS
     TEKIAVYTTR PDTVYGVSYV VLAPEHPLTK QVTSKTQQAV VDTFIQEVTN QSELERTAED
     KPKRGVATGG KAINPFTGEE VPIWIADYVL YEYGTGAVMG VPAHDVRDFK FAQRYDLPID
     FVIAAPDDVA GFDLSPTSET EEVTQVVQIE YNQAYTEPGI LINSGAFTGM TSTDAKQAIV
     KYATEKGFGK ERIQYRLRDW LISRQRYWGA PIPVIHCPNC GIVPVPDKDL PVILPEEVEF
     TGRGGSPLAQ LESWVNVPCP TCGSPAKRET DTMDTFIDSS WYFLRFTDAR NEAQVFESAK
     TNDWMPVDQY VGGIEHAILH LLYSRFFTKV LRDRGLLNFD EPFERLLTQG MVQGLTYFNP
     NKGGKDKWVP SHLVNPNDPR DPQTGEPLQR LYATMSKSKG NGVAPEDVIA KYGVDTARMF
     ILFKAPPEKD LEWDEADVEG QFRFLNRVWR LVTDYVASGV NPKNKSGELS KSEKDLRRAI
     HSAIQSVTED LEDEYQFNTA ISELMKLSNA LTDANGKDSR VYAEGIHTLV VLLAPFAPHI
     AEELWQLLGN SESVHTQTWP AFDPAALVAD EITLVIQVNG KKRADIQVPS QADKAELEKY
     ARESEVVQRH LEGKEIKKVI VVPGKLVNFV VG