ID   SYL_STAMF               Reviewed;         969 AA.
AC   A3DKS1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=Smar_0118;
OS   Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Staphylothermus.
OX   NCBI_TaxID=399550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX   PubMed=19341479; DOI=10.1186/1471-2164-10-145;
RA   Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I.,
RA   Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A.,
RA   Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B.,
RA   Woese C., Bristow J., Kyrpides N.;
RT   "The complete genome sequence of Staphylothermus marinus reveals
RT   differences in sulfur metabolism among heterotrophic Crenarchaeota.";
RL   BMC Genomics 10:145-145(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX   PubMed=21304655; DOI=10.4056/sigs.30527;
RA   Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986
RT   type strain F1.";
RL   Stand. Genomic Sci. 1:183-188(2009).
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; CP000575; ABN69231.1; -; Genomic_DNA.
DR   RefSeq; WP_011838422.1; NC_009033.1.
DR   AlphaFoldDB; A3DKS1; -.
DR   SMR; A3DKS1; -.
DR   STRING; 399550.Smar_0118; -.
DR   GeneID; 4906962; -.
DR   KEGG; smr:Smar_0118; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OrthoDB; 23906at2157; -.
DR   Proteomes; UP000000254; 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   CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR   Gene3D; 3.30.2320.20; Class I aminoacyl-tRNA synthetases (RS); 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.10.720; leucyl-tRNA synthetase; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   NCBIfam; TIGR00395; leuS_arch; 1.
DR   PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..969
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334848"
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT   MOTIF           649..653
FT                   /note="'KMSKS' region"
FT   BINDING         652
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   969 AA;  113418 MW;  F8EFAE27BDF6D1AB CRC64;
     MKKRDFLEWL RSVEAKWQSK WMEKKIFEPR IEPDKPKYFI TVPYPYTNAP LHIGHGRTYT
     IGDIIARYKR LRGYNVLFPM AFHITGTPII AISERISRGE EEIINRYKSY IAKYVKDPVE
     IEKIIESFKD PLNLAVFFAE RVHMDFDALG YSIDWRRRFH TGEPIYNAFV TWQFLKLREK
     GLIKRGDHVV TYCLLHKQPE GEDDIQDADV NPVEILEFTA IKFKLLGEEN TYLVAATLRP
     ETLFGATNLW VKPDADYVVV EWRGENIIVS KEALVKLQHQ HPLDEFKVVG EMKGRELVGK
     KVVSPLGNEL IVLPADFVDP DNATGIVYSE PSDAPYDYVA LMELKKNSEK LAMYGVDPEV
     VKKIEPIKII DVPGIKGHHA GIVVEEMGIS SQFDPRLVEA TKIVYREQYY KGVMIVDDPE
     FKGLSVSEAK EKIKKKLLRE NKGFVFYELN RKAYCRAGGK IIAAKIIGQW FIDYSVPWWK
     EEAKKYVSEK MRIIPVKYKK AMLDAIDWLE RRPCARKRGL GTRLPFDPEW VIESLSDSTI
     YMAFYTIAHL IRKHNIKPEQ LKPQVFDYVF LGKGDPEEIS EDTGIPLKAL EEMRQEFNYW
     YPVDQRHTGI AHISNHLSFF IYHHIAIFPR KHWPKMITLN EMVIREGTKM SKSKGNVILL
     RDIAEKYSAD LFRLYIAGAA NLDTVLDWRE KEVERVIDSL KKFTAIAEKA IRTKCGTYSH
     DKYIDKWFLS KFNRLLAEAT NALDNMEIRD YVQKMFYDVM VSIDHYRERT SNEETICMIK
     RILSKWLKSL NPVIPHLTEE IWSWMGKEEF LSLEKWPEID YKAINEEVEY LEEAIEALIE
     DIKNVLNILS PKPKHAYIVV ASPWKREVIE MIEKGMDRRE IIRTIRDKYG LKGREKEIVY
     VIQECSRTPC KRALKIDPIH EYEAYNEARQ YIAKKTGLHI EVYWEEEAKA KNIPKAEKTL
     PLKPSFYLY
//