SYL_METMA
ID SYL_METMA Reviewed; 966 AA.
AC Q8Q054;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
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=MM_0283;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM29979.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008384; AAM29979.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048038036.1; NC_003901.1.
DR AlphaFoldDB; Q8Q054; -.
DR SMR; Q8Q054; -.
DR STRING; 192952.MM_0283; -.
DR PRIDE; Q8Q054; -.
DR EnsemblBacteria; AAM29979; AAM29979; MM_0283.
DR GeneID; 44086522; -.
DR KEGG; mma:MM_0283; -.
DR PATRIC; fig|192952.21.peg.347; -.
DR eggNOG; arCOG00809; Archaea.
DR HOGENOM; CLU_004174_0_0_2; -.
DR OMA; AWNMAFQ; -.
DR Proteomes; UP000000595; 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; -; 1.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_00049_A; Leu_tRNA_synth_A; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR020791; Leu-tRNA-lgase_arc.
DR InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; PTHR45794; PTHR45794; 2.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00395; leuS_arch; 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..966
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152133"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT MOTIF 632..636
FT /note="'KMSKS' region"
FT BINDING 635
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 966 AA; 110957 MW; 561D0FDC574A0DC3 CRC64;
MEQDYKPHEI ENKWQKKWNE SRIFQAEPDK REKFFITIPY PYLNGNLHAG HTRTFTIGDV
VARHKRMLGY NVLYPMGFHV TGTPIVGLAE LIASRDPQTM DVYERLHGIP GDILPALDTP
EKIVDYFKVE AEKAMRMIGY SIDWRRKFTT TDPTYKKFIE WQYTRLEEKD LIVKGSHPVK
WCPNDNNPVE DHDILHGEEA TIVEYTLIKF RYRDLVLPCA TLRPETTYGV TNLWVNPNVD
YVKARVEKDG NVEFWVVSRD AFRKLTFTDR TVEYVEDMPA KSIIGIKLTN PVTGDEVISL
PASFVKPENG SGIVMSVPAH APFDYLALRD LYDADLSEYG ITEDLRKIEL ISLIQVPEFG
EFPAKEIVES MGISDQKDPK AEEATKIVYR REFHGGVLKE LTGKYKGYPV SKIKDILTRD
FLASNAGETF YEFSEPVVCR CGTPCVVNMV KGQWFLNYSN PDWKAKVYKC LGQMRVIPTE
YRVEFENKID WLKDKACARR KGLGTRLPFD KEWLIESLGD STIYMSYYII ARFIEKGELA
LEHLTLSFFD YVLLGKGDSA AVSAETGLKP ELIEEIRSHF NYWYPVDLRS SGKDLVPNHL
LFFLFHHVAL FEEEKWPKAL AVNGFVSLEG QKMSKSKGPI LTLESAVSSY GADITRMYIL
STAEQTQDAD WQKAGIDSAR RQVDRFYAFA KDVIESGKRG TLSAELKQID RWMLSRMQNY
IKETNAALDS IQTREAIQNS FFLLINDVRW YQRRGGEALL YYVLDNWVRL MAPFTPHLCE
EVWEAMGHED PVSLAQYPLY NEDLIDNGAE LSEEAVKSTL NDIEEIIRVT KMTPQKVYLY
TAPAWKAEAI RCACGLQVEA PLEVGTLIKT LMAKPELKRF GKEIPKFVQK IVPEFKSGGA
ERYETFAYLG LDEKDLLKES ASFLEKEIGC PVEIQSADSP EYDPQKKSRF AEPLRPAIYI
EEKKEE