SYL_NOSS1
ID SYL_NOSS1 Reviewed; 872 AA.
AC Q8YS09;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, 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=alr3283;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; BA000019; BAB74982.1; -; Genomic_DNA.
DR PIR; AD2216; AD2216.
DR RefSeq; WP_010997434.1; NZ_RSCN01000001.1.
DR AlphaFoldDB; Q8YS09; -.
DR SMR; Q8YS09; -.
DR STRING; 103690.17132378; -.
DR EnsemblBacteria; BAB74982; BAB74982; BAB74982.
DR KEGG; ana:alr3283; -.
DR eggNOG; COG0495; Bacteria.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002483; 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; Reference proteome.
FT CHAIN 1..872
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000151961"
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; 98549 MW; A7B4CAD72C643C0C CRC64;
MDSRYNPATL EEKWQKTWVE LGLDKTQTQS NKPKFYALSM FPYPSGSLHM GHVRNYTITD
VIARLKRMQG YRVLHPMGWD AFGLPAENAA IDRGVPPAKW TYQNITQMRQ QLQRLGLSID
WDSEVATCSP DYYKWTQWIF LQFLQAGLAY QKEAAVNWDP IDQTVLANEQ VDNEGRSWRS
GAIVERKLLR QWFLKITDYA EELLNDLDKL TGWPERVKLM QANWIGKSSG AYLEFPIVGS
NEKIAVYTTR PDTVYGVSYV VLAPEHPLTK QVTTKTQQAA VDTFIQEVTN QSELERTAED
KPKRGIATGG KAINPFTGEE VPIWIADYVL YEYGTGAVMG VPAHDVRDFK FAQRYDLPID
FVIAAPDDVA GFDLSPTSET EEVTQVVQIE YNQAYTEPGI LINSGAFTGM TSTDAKQAIV
KYATEKGFGK ERIQYRLRDW LISRQRYWGA PIPVIHCPNC GIVPVPDKDL PVILPEEVEF
TGRGGSPLAQ LESWVNVPCP TCGTPAKRET DTMDTFIDSS WYFLRFTDAR NEAQVFESAK
TNDWMPVDQY VGGIEHAILH LLYSRFFTKV LRDRGLLNFD EPFERLLTQG MVQGLTYFNP
NKGGKDKWVP SHLVNPNDPR DPQTGEPLQR LYATMSKSKG NGVAPEDVIA KYGVDTARMF
ILFKAPPEKD LEWDEADVEG QFRFLNRVWR LVTDYVASGV NPKNKSGELS KSEKDLRRAI
HTAIQSVTED LEDDYQFNTA ISELMKLSNA LTDANGKDSR VYAEGIKTLV VLLAPFAPHI
AEELWRLLGN SESVHTQTWP AFDPAALVAD EITLVIQVNG KKRADIQVPS QADKAELEKY
ARESEVVQRH LEGKEIKKVI VVPGKLVNFV VG