SYL_HALOH
ID SYL_HALOH Reviewed; 830 AA.
AC B8CXR8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Hore_13370;
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562;
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(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; CP001098; ACL70087.1; -; Genomic_DNA.
DR RefSeq; WP_012636271.1; NC_011899.1.
DR AlphaFoldDB; B8CXR8; -.
DR SMR; B8CXR8; -.
DR STRING; 373903.Hore_13370; -.
DR PRIDE; B8CXR8; -.
DR EnsemblBacteria; ACL70087; ACL70087; Hore_13370.
DR KEGG; hor:Hore_13370; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000719; 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; -; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
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 PANTHER; PTHR43740; PTHR43740; 2.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 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..830
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000199209"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 585..589
FT /note="'KMSKS' region"
FT BINDING 588
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 830 AA; 96269 MW; 9BB05557D27E2CE8 CRC64;
MKGYYNFADI EKKWQDKWEK DGLYKTQEET DKDNYYVLEM FPYPSGNLHM GHVRVYSIGD
VIARFKRMNG YNVLHPMGWD AFGLPAENAA IKHGNIHPQD WTWDNIKNMK KQMKSLGLSY
DWDREVTTAK EDYYKWTQWF FVKMFKKGLA YKKKAAVNWC PGCETVLANE QVVNNACERC
GTEVEEKELE QWFFKITNYA ERLLEDHKLL QNWPEKVKIM QRNWIGRSEG MRIKFPVKGS
SEEIEVFTTR PDTIFGATYM VLAPEHPLVE KLISGTEKEK EVRQFIDRVK KQKEMERTSP
ESEKEGLFTG AYAINPMTGE EIPIMIANYV LMGYGTGAIM AVPAHDQRDF DFARKYDLPI
RVVIQPEERE EELKDTDLNE AYEGSGHLIN SDKYNGLTVK EAFDVMAEDM EKEGIGKREV
NYRLRDWLIS RQRYWGTPIP IVYCEKCGTV PVPEEELPVV LPRDVEFSPT GESPLAKVDE
FVNTTCPVCG GKARRETDTM DTFVDSSWYF LRYTDPKNDK LPFSKENAKK WFPVDQYIGG
IEHAILHLLY ARFFTKVIYD MDMIDSVEPF TNWLAQGMVL KDGAKMSKSK GNVVDPEDIL
DRFGADTARL FILFAAPPEK DLEWSDRGVE GAERFLNRVW RLVADNIKEI KNTDQASLDV
NSFNKNEKDL YRNLHVTIKR VTEDIGERLN FNTAISAIME LTNATYQYLN GVEKVNYTLI
KDIIEKMLLI LAPFAPHMTE ELWSELGNDE SIHIQKWPGY EEKALKKDEV TIVVQVNGKV
RDKLQVSADI DEDKLKEQVL ELPRIQKYTE GKEIVKTIII PKKLVNIVVK