SYL_THEAC
ID SYL_THEAC Reviewed; 910 AA.
AC Q9HK31;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=Ta0777;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL445065; CAC11908.1; -; Genomic_DNA.
DR RefSeq; WP_010901190.1; NC_002578.1.
DR AlphaFoldDB; Q9HK31; -.
DR SMR; Q9HK31; -.
DR STRING; 273075.Ta0777; -.
DR PRIDE; Q9HK31; -.
DR EnsemblBacteria; CAC11908; CAC11908; CAC11908.
DR GeneID; 1456331; -.
DR KEGG; tac:Ta0777; -.
DR eggNOG; arCOG00809; Archaea.
DR HOGENOM; CLU_004174_0_0_2; -.
DR OMA; AWNMAFQ; -.
DR OrthoDB; 4914at2157; -.
DR Proteomes; UP000001024; 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..910
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152148"
FT MOTIF 50..60
FT /note="'HIGH' region"
FT MOTIF 611..615
FT /note="'KMSKS' region"
FT BINDING 614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 910 AA; 105028 MW; 17FA01BB946DF0BE CRC64;
MDDRGRRCCT HSGVIALDIE AKWQNAWDRD GIFVPKMDGR KKFMITVPWP YTNGSLHVGH
GRTYTLGDII ARYKRSRNYN VLFPMGFHQS GTPILAFSER IRAGDRSTID LYTSYLKEYG
EKDIDALIES FKDPKNIADY FSNAIINDFK HLGYSIDWTR RFTSADEFYQ KFVQWQFRRL
NEKGLVKQGR YPILYSLEDD NAVGEDDIKD GDTDKVTIEE YTAIFFRGKS FDLIAASLRP
ETIYGITNIW VNPDVKYVKV KISGRMAVVS EECSTKLKFQ GNEIEVAGEA SVQEIQKQTY
TTPAGKEVKV YQADFVDPDN GTGIVYSVPS HSVYDYVYYR KKRGKDFPVI IEAPMKMKDI
ESKYDLETEE GREEATKDLY RNEFYYGKLV DSGPYTGMTV REAREAVKRD LISSGNAFTF
YETSRHAVTR SGSKVIVAVL PDQWFLDYSQ PWLKDLGHTM INTMTMHPEV YRNVMNDAID
WLKERPCARR RGLGTRLPFD DRWVIESLSD STIYPAVYTN SIPLRSLYET GKLDDDAITR
IFMNGEPKNE DESEAKRQFE YWYPVDIRLT AIPHISNHLS FYVLNHAAIF PKEKWPAGLI
ISGLVVSNGA KISKSKGNVV SLLEIAKKYS ADIYRLYVAV QADISSTMDW NETDLASITR
RFNEFKDLMA GFKQDTSDLT FEEAWFVARF SVRLRQFMES MDRYQIRDAY INIFYGVLND
LRYLSSRGGD VNRALTPVIA DWLRALMPVI PHHAEEYWHS YVSDTYVSVD PFDENFQDRY
ERTVRRFGMT CDQMYSAMDY VEKVLQDVKN IMQVTGIEPK SVEITVANAD VVRAAQEFLN
NSVSGQSKKY MQYLAKRRKD IMIYGFDEYD VLQRNQVYLS KQIGCPVRIE RGDVINGKIA
LPGKPVIYIS