ID SYL_PYRIL Reviewed; 945 AA.
AC A1RTX9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
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=Pisl_1246;
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000504; ABL88411.1; -; Genomic_DNA.
DR RefSeq; WP_011762986.1; NC_008701.1.
DR AlphaFoldDB; A1RTX9; -.
DR SMR; A1RTX9; -.
DR STRING; 384616.Pisl_1246; -.
DR GeneID; 4616435; -.
DR KEGG; pis:Pisl_1246; -.
DR eggNOG; arCOG00809; Archaea.
DR HOGENOM; CLU_004174_0_0_2; -.
DR OrthoDB; 23906at2157; -.
DR Proteomes; UP000002595; 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; cd00812; LeuRS_core; 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.
FT CHAIN 1..945
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009405"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 638..642
FT /note="'KMSKS' region"
FT BINDING 641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 945 AA; 107947 MW; 66351DCA0CEB630D CRC64;
MSELSRFFIE IAERWQKRWK ESRVFEPEPT PGVAKYFITA AYPYPNGAVH IGHGRTYLIA
DVLARFYRHM GRVVLYPMGF HYTGTPILTI AEVIAAGDKT VIEEYMEIYG VPEEEIKKMG
DPLYLARYFH NRSKMAMERF GLSIDWTREF TTIDPEYQRF IQWQFEKLRK KGLIVRGRHP
VGWCPRHSMP VGAHDTKDDK EPEIGQWTLI YFTDSEGLTF PAATLRPETV PGVTNLWINP
DAEYVVAEFD GKRVVISRDA AYRLSFQAEV KILREARGRE FVGRSVQNPV TGEWVPIYEA
WFVDPRVGTG VVMSVPAHAP YDYVALRDLG IEKLIPLIKV EGYGDYPAKE VVERMGIKSQ
TDPALEEATK EVYSTEYTRG VMREDVTERI GIHLQEPARS MLRAVFKMYF AGRPVREARE
FIAKWLVEAR LGGVMYDIMN KPVYCRCGTE IVVKVLEDQW FINYGDPKWK ETARKLVDEM
VIIPGEAKAH FFATIDWLDK RACARTRGLG TPLPWSSGWI IESLSDSTIY MAFYTVIKKI
RQFGIRPEQL TEEFWDFVFL GQGSADEVSK KTGVPVEALK AIREEFEYWY PLDSRNSGKD
LIPNHLTFFI FNHVAIFPRE KWPRQIVANG WVLREGEKMS KSKRNVLPLD RAVEMYGPDP
LRATLALAAE VEQDLDFRDA EARRNAQQLM AIYTLVQRLI QNAENRPAGW IDQWLIAEIS
RILDKAREAY EKVRVRQAAV EVIYNAKAVF DQYLAMVEKP TKLALEAARA WVVAMEPIVP
HIAEELWALL GGSGFVATAP WPRLKAESAA LLAKRYVDML IEDVKNIPAF GPGARRIVIY
VNRNFSWAKA ALNGDVKTVV TAGAPPQVAK RLIDLVKTLG DEVRTLLAST EQFDELETLK
SYKAYIERTL GTPIEIYSVD DPSAPDLGGK KRAALPLKPG IYIER
//
