SYL_RHOBA
ID SYL_RHOBA Reviewed; 950 AA.
AC Q7UMC0;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, 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=RB8919;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294148; CAD75997.1; -; Genomic_DNA.
DR RefSeq; NP_868620.1; NC_005027.1.
DR RefSeq; WP_011122073.1; NC_005027.1.
DR AlphaFoldDB; Q7UMC0; -.
DR SMR; Q7UMC0; -.
DR STRING; 243090.RB8919; -.
DR PRIDE; Q7UMC0; -.
DR EnsemblBacteria; CAD75997; CAD75997; RB8919.
DR KEGG; rba:RB8919; -.
DR PATRIC; fig|243090.15.peg.4279; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_0; -.
DR InParanoid; Q7UMC0; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR Gene3D; 3.40.50.620; -; 3.
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; 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 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..950
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152072"
FT MOTIF 41..52
FT /note="'HIGH' region"
FT MOTIF 718..722
FT /note="'KMSKS' region"
FT BINDING 721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 950 AA; 107071 MW; 7CB553E51E6DA6B6 CRC64;
MVRYNPNEIE PRWQAYWDEH HTFATPEKVG KKKRYVLDMF PYPSGDGLHV GHPEGYTATD
IVSRFARARG ESVLHPMGFD AFGLPAEEHA IKTGEHPRVQ TQRNIDNFTR QLKMLGFSYD
WDRVLATTDE EYFRWTQWIF GVLYDTWFDH DQQKGRPISE LPIPAEVTAE GELEIEQYRD
SKRLAYLDDA LVNWCPKLGT VLANEEVVDG KSEVGGHPVK RIPLRQWMLR ITDYAERLLD
GLDDLDWPTG IKKLQSDWIG RSTGGEVDFY LQRGAAGDDT GPFVAFKRAR ESEGFPTDPG
KDCLRVYTTR PDTLFGATYM VVAPEHPLID VLVKPEQKDE VDAYREKASF KSDRERTDGD
RAKTGVFTGS YAINPADGRS IPIWVADYVL AGYGTGAIMA VPAHDERDFE FAVAFDLPVI
PVVDPPADHK QREEILAGKA CFAAEGVAIN SGEYDGKTTA EVKAALTAEL AKQGLACEAV
NYKLRDWLFS RQRFWGEPFP VLHEIDSEGN ATGVRRLVPD DQLPVTLPEL ADFKPHGRPE
PPLAKADDDW LIVELDGKRY RRETNTMPQW AGSCWYYLRY IDPKNSDALI DPQKEKDWMP
VDLYVGGAEH AVLHLLYSRF WHKVLFDRGH VTCPEPFGKL VNQGMILGEV EFTSFVDPSG
KHVSTKDVKK DAEGNRVHKA TGEQVEIVSL TEEQVVKKGE GFVLASDASI KVDSRAFKMS
KSRGNVVNPD SVVRDYGADS LRLYEMFMGP LEATKPWAMN GVGGVRSFLD RVWRMIIDEP
EDELKVSDAV VDTACDEEQL RVLHQTIRKV TEDNEAMSFN TAIAKMMEFT NHFTRCETRP
REAMESFLIL LAPYAPHMCE ELWKHLGHNE SISLQPWPKW DEAALVQSSI EIPVQINGKV
KAKISLSPDA KPNEMGEAAL ADPAVQNAIG DKKVVKTIAV PGRMVNLVVK