ID D5U115_THEAM Unreviewed; 968 AA.
AC D5U115;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=Tagg_0541 {ECO:0000313|EMBL:ADG90815.1};
OS Thermosphaera aggregans (strain DSM 11486 / M11TL).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Thermosphaera.
OX NCBI_TaxID=633148 {ECO:0000313|EMBL:ADG90815.1, ECO:0000313|Proteomes:UP000002376};
RN [1] {ECO:0000313|EMBL:ADG90815.1, ECO:0000313|Proteomes:UP000002376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376};
RX PubMed=21304709;
RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL).";
RL Stand. Genomic Sci. 2:245-259(2010).
RN [2] {ECO:0000313|Proteomes:UP000002376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376};
RX DOI=10.4056/sigs.821804;
RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.C., Brettin T.,
RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain
RT (M11TLT).";
RL Stand. Genomic Sci. 2:245-259(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 11486;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Spring S., Lapidus A., Munk C., Schroeder M., Glavina Del Rio T., Tice H.,
RA Copeland A., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J.,
RA Jeffries C.C., Brettin T., Detter J.C., Tapia R., Han C., Chain P.,
RA Heimerl T., Weik F., Goker M., Rachel R., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL).";
RL Submitted (FEB-2010) 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:RU363035}.
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DR EMBL; CP001939; ADG90815.1; -; Genomic_DNA.
DR AlphaFoldDB; D5U115; -.
DR STRING; 633148.Tagg_0541; -.
DR KEGG; tag:Tagg_0541; -.
DR eggNOG; arCOG00809; Archaea.
DR HOGENOM; CLU_004174_0_0_2; -.
DR Proteomes; UP000002376; 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; 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; 2.
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 {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:UP000002376}.
FT DOMAIN 19..527
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 594..683
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 726..850
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 651..655
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 654
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 968 AA; 112296 MW; 4BF70240C1753837 CRC64;
MITLDKKDFL EWMRSIEAKW QKKWKEAGVF EPKVEESKVK YFLTVPYPYT NGPLHIGHGR
TYTIGDIIAR FKRLTGYNVL FPMAFHITGT PIIAISERIA NKDAKTLDMY RSYISYYIED
REKVEEILES FKDPLKLATF FAEKVQSDFE ALGYSIDWRR KFHTGEPIYN AFVTWQYNRL
RQLGVVAKGE HMVTYCLLHK QPEGEDDIQD ADVNPVEILE YTAIKFKLEG SESSLLASTL
RPETLLGATN IWVNPEAEYV IVEFNGERLI ISKKAWVKLA HQHVESDIRI LGELKGSELI
GKTVESPLGQ KLLVLPAAFV DPDNATGIVY SEPSDAPYDY VALIELKANP HLLEAYGMDA
RIVENINPIK IIEVPGIADH HAKAVVEKYG ITSQLDDRLE EATREVYREQ FYNGKLIVDH
PDFKGLSVPE AREKMKKKLI SDGKAMVFYE LNRRAFCRGG GEIIVAKIRD QWFIDYSVPW
WKDRTRNLIN ERLEIIPPKY KKAFQDVLEW VEKRPCARKR GLGTKLPWEP DWIIESLSDS
TIYMAFYTIA HKIREYRIPP EKLIPAFFDY VFLGEGCAEE ISKETGIPVE LIEEMRKEFN
YWYPVDHRHT GIPHISNHLT FYLFHHTAIF PEDKWPRIIS LNETVIREGA KMSKSKGNVI
PLRDIARNYS ADLFRFYIAS AASLDSVLDW KQKEIELVLD GLYRFTNIML QARSIGGEIP
SDFYGRWFAS KFRRIISDSR KSMELLEVRD YVQKAFYHVM NLIEQYRDLV GENYLKAVKY
ISKDWLIMLN PVIPHLTEEL NELLGGSGFL STSEWPTGSR YWEDEESEIL VDSLFALVED
VKKILEVLKK PATKAVIIVA PEWKREALKL YREGKGIKSI IEELKSKYNL RGRELEIVET
VQTFSKNPNE DVFKTSSKRE YEVLEYSVNF LERKTGLKIE VLWEDEARAR GIPRSEKAQP
LKPAIYVD
//
