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Database: UniProt
Entry: L0AB07_CALLD
LinkDB: L0AB07_CALLD
Original site: L0AB07_CALLD 
ID   L0AB07_CALLD            Unreviewed;       956 AA.
AC   L0AB07;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   OrderedLocusNames=Calag_0458 {ECO:0000313|EMBL:AFZ70225.1};
OS   Caldisphaera lagunensis (strain DSM 15908 / JCM 11604 / ANMR 0165 /
OS   IC-154).
OC   Archaea; Thermoproteota; Thermoprotei; Acidilobales; Caldisphaeraceae;
OC   Caldisphaera.
OX   NCBI_TaxID=1056495 {ECO:0000313|EMBL:AFZ70225.1, ECO:0000313|Proteomes:UP000010469};
RN   [1] {ECO:0000313|Proteomes:UP000010469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15908 / JCM 11604 / IC-154
RC   {ECO:0000313|Proteomes:UP000010469};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete genome of Caldisphaera lagunensis DSM 15908.";
RL   Submitted (MAR-2012) 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:0000256|HAMAP-Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00049, ECO:0000256|RuleBase:RU363039}.
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DR   EMBL; CP003378; AFZ70225.1; -; Genomic_DNA.
DR   RefSeq; WP_015232123.1; NC_019791.1.
DR   AlphaFoldDB; L0AB07; -.
DR   STRING; 1056495.Calag_0458; -.
DR   GeneID; 14211718; -.
DR   KEGG; clg:Calag_0458; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   InParanoid; L0AB07; -.
DR   OrthoDB; 23906at2157; -.
DR   Proteomes; UP000010469; 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; 3.30.2320.20; 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; 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; 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   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   Pfam; PF09334; tRNA-synt_1g; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00049};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00049}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00049};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00049}; Reference proteome {ECO:0000313|Proteomes:UP000010469}.
FT   DOMAIN          17..517
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          595..699
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          714..843
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   MOTIF           639..643
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         642
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   956 AA;  112118 MW;  9BBF043CCD08E672 CRC64;
     MEDKNEIINN LKEIESKWQN KWSESKIFEA NPDENKKKFF ITFPFPYMNG LPHLGSAFTI
     LRVDVMARYK RMRGYNVLFP QGWHATGGPI VASARRIKEN DTKKIQELKS MGVPDELIKN
     FEEPSYWVYY FTNEWEKDLK RYGLSIDWRR KFFTTNLNPY FSKFVEWQYY KLRERNYVTK
     GSHPVVWCPK EKKVVGDHDR PDEYAGIGPI DATIIKFKME DGKIIPTLTY RPETIFGVTN
     IWINKDYMYN IAEIDGEIWI INDYMAEELA DQKHEVKLIQ KINGKELIGK YAINPINNKK
     VLILPAEFVI PDEGTGIVMS VPAHAPYDYV ALEDLKINKK LIKELNLNEE EINKLTPIQI
     IKTAEFKDIP AKEITKKLGI KNQNNVELLE KATKELYAKE FYNGIMYNVD SKYTNLKVNE
     AKELIASDLR NENKALKVYT LPSKVYCRCG ARTHIKFVEN QWFLLYSNEE WKSKAREIVK
     NMNFYPESAK DDFLRLVDWL NDWACTHMNE LGTPLPWDKN WVIESLSDST IYMAYYTISH
     FIQNKVDPSN LIPELFDYIF LGIGDLDEIS KKTHLDKNFI ESMRKEFLYW YPVDLRISGK
     DLIQNHLLFF IYHHAAIFDK ERWPKGIGIN GWVLLNGEKM AKSKGNFLLL RDALNKWGAD
     VTRWSEIMAG ADPGYDDANF ESSLVENAIE ELNTWLNFVK NNYNKGRDYR LSLDYWFESI
     INSTIKEVTE DMEKTRFKSA LIKSYYYLKN KYKWYLTRSN VPNKEVVNKY LETVTLMIAP
     IAPHVAEEAW HLMGHNDFVS LHSWPEADES KINKDYEKSE ELIEKIINDS KELISLIGDA
     KKVHIIIASP WKYELFNDAK SKMKNKSLKE LRSELIKNDY KVEKGKVAKV IDMISKYPEL
     LENYISRDLE IKSIQESKDF LEKELNKEIS IALEENSNLP RSDLALPGRP ALYLEK
//
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