SYL_STAMF
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 03-AUG-2022, entry version 94.
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=Smar_0118;
OS Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC Archaea; Crenarchaeota; 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 EnsemblBacteria; ABN69231; ABN69231; Smar_0118.
DR GeneID; 4906962; -.
DR KEGG; smr:Smar_0118; -.
DR eggNOG; arCOG00809; Archaea.
DR HOGENOM; CLU_004174_0_0_2; -.
DR OMA; AWNMAFQ; -.
DR OrthoDB; 4914at2157; -.
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 Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.740.10; -; 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 PANTHER; PTHR45794; PTHR45794; 2.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00395; leuS_arch; 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
