SYL_CERS4
ID SYL_CERS4 Reviewed; 847 AA.
AC Q3IZL4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=RHOS4_24520;
GN ORFNames=RSP_0840;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000143; ABA80020.1; -; Genomic_DNA.
DR RefSeq; WP_011338533.1; NZ_CP030271.1.
DR RefSeq; YP_353921.1; NC_007493.2.
DR AlphaFoldDB; Q3IZL4; -.
DR SMR; Q3IZL4; -.
DR STRING; 272943.RSP_0840; -.
DR EnsemblBacteria; ABA80020; ABA80020; RSP_0840.
DR KEGG; rsp:RSP_0840; -.
DR PATRIC; fig|272943.9.peg.2803; -.
DR eggNOG; COG0495; Bacteria.
DR OMA; TFMVLAP; -.
DR PhylomeDB; Q3IZL4; -.
DR Proteomes; UP000002703; Chromosome 1.
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 Gene3D; 3.90.740.10; -; 1.
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; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
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..847
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009414"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT MOTIF 619..623
FT /note="'KMSKS' region"
FT BINDING 622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 847 AA; 94033 MW; E52C27363BB7CAC6 CRC64;
MSRYDPAATE SRWQAAWDAA GVFTARHDPA RPKYYVLEMF PYPSGRIHMG HVRNYTMGDV
VARQKAAAGF SVLHPMGWDA FGMPAENAAM ERGGHPKDWT YGNIADMRAQ MKPLGLSIDW
SREFATCDPE YYGQQQAMFI DMMEAGLVYR KNAVVNWDPV DMTVLANEQV IDGKGWRSGA
PVVRRELTQW FFRISDYAGE LLEALDTLKD WPEKVRLMQA NWIGQSRGLQ FAFSMAGAPE
GFDRLEVYTT RPDTLMGASF AAISPDHPLA RHLERHDPEV AEFVAECRRV GTSEEALEKA
EKKGFDTGLR VRHPFDAAWE LPVYIANFIL MDYGTGAIFG CPAHDQRDFE FATKYGLPIR
PVFLPEGCEE TALAEAFVPM KSERVHYIRG FAGAEVQTGE EGVAAAIAFC ESQGVGRGVT
NYRLRDWGIS RQRYWGCPIP VIHCETCGVV PEAKENLPVR LPDDVSFDVP GNPLDRHPTW
RDCTCPKCGA KARRETDTMD TFVDSSWYYA RFTAPRAATP TDAEEADYWM NVDQYIGGIE
HAILHLLYSR FFARAMQKTG HLPAKAIEPF NALFTQGMVT HEIYLTRDAA GRPVYHLPED
VTDGKLADGT PVEIIPSAKM SKSKKNVVDP MNIIRQFGAD TARWFVMSDS PPERDVEWTA
SGAEAASKHL HRVWRLADEI SRADGEANAE DGALDKATAR AIAEVTQGVE GFAFNKAIAK
LYEFTNTLSR SGAGAEAKKR AMRTMAQLMS PMVPHLAEEV WAMLGGEGLV AQAAWPKADP
ALLIDDTVTL PIQVNGKRRG EITVPKEMAA SEVEKLVLAD EAVQRALGGA APKKLIVVPG
RIVNVVI