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A5HY79 (SYL_CLOBH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucine--tRNA ligase

EC=6.1.1.4
Alternative name(s):
Leucyl-tRNA synthetase
Short name=LeuRS
Gene names
Name:leuS
Ordered Locus Names:CBO0186, CLC_0240
OrganismClostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) [Reference proteome] [HAMAP]
Taxonomic identifier441771 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length813 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). HAMAP-Rule MF_00049

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00049.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processleucyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

leucine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 813813Leucine--tRNA ligase HAMAP-Rule MF_00049
PRO_1000009326

Regions

Motif40 – 5112"HIGH" region HAMAP-Rule MF_00049
Motif572 – 5765"KMSKS" region HAMAP-Rule MF_00049

Sites

Binding site5751ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5HY79 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: F4DECBDF3244DC0D

FASTA81392,912
        10         20         30         40         50         60 
MGNYSTKIDE KWQKKWEENS LYKFNNKNLD KKLYVLEMFS YPSGSKLHAG HWFNYGPVDS 

        70         80         90        100        110        120 
WARFKRMQGY NVFQPMGFDA FGLPAENYAI KTGIHPKDST FKNIETMETQ LKAMGAMFNW 

       130        140        150        160        170        180 
ENEVITCSPD YYKWTQWLFL KLYEKGLAYK KKAPVNWCPS CNTVLANEQV LDGKCERCDS 

       190        200        210        220        230        240 
NVDKKNLEQW FLKITDYADE LLEKLDELDW PEKTKAMQKH WIGKSVGAEV TFNVADSDLS 

       250        260        270        280        290        300 
FNVFTTRVDT LFGVTYVVLA PENDLVDKLT TPENKAEVES YKTQAKNQSD IERQSITREK 

       310        320        330        340        350        360 
TGVFSGSYAI NPINGKKVPI WIGDYVLNTY GTGCVMAVPA HDERDFAFAT KYNLPIERVI 

       370        380        390        400        410        420 
EGGDSLPYTE YGGMVNSGEF DGLLGNEAKE AVISKLESMN LGRKKINYRL RDWLVSRQRY 

       430        440        450        460        470        480 
WGAPIPIIYC EKCGTVEVPI EQLPVELPYN VEFSPDGKSP LGKCDDFINT TCPKCGGPAK 

       490        500        510        520        530        540 
READTLDTFV CSSWYYLRYP DNNNEKDAFN PELINKMLPV DKYVGGPEHA CMHLLYARFI 

       550        560        570        580        590        600 
TKALRDMGYL NFDEPFLSLT HQGLILGPDG LKMSKSKGNT ISPDDYIKEF GADVFRMYLM 

       610        620        630        640        650        660 
FGFDYTEGGA WSDDAIKSIG KFVDRVERIL ENAREEIKNS KDNKSTMDKD EKELNYVRHH 

       670        680        690        700        710        720 
SIKSITEDID KMQFNTSIAR LMEFTNALSK YLGIDAIKNA LFLRESIIDF ITLLAPFAPH 

       730        740        750        760        770        780 
FAEEQWKLIG INSSIFNEKW PEFDPKALIK DEVEIAVQVN GKIRAKINIS TSSSEDEIKE 

       790        800        810 
SALNNEDIKN SIGDKEIKKV IVIKNRLVNI VAK 

« Hide

References

[1]"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes."
Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. expand/collapse author list , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J.
Genome Res. 17:1082-1092(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.
[2]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000727 Genomic DNA. Translation: ABS36860.1.
AM412317 Genomic DNA. Translation: CAL81738.1.
RefSeqYP_001252730.1. NC_009495.1.
YP_001386143.1. NC_009698.1.

3D structure databases

ProteinModelPortalA5HY79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING413999.CBO0186.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS36860; ABS36860; CLC_0240.
GeneID5187707.
5400866.
KEGGcbh:CLC_0240.
cbo:CBO0186.
PATRIC19362465. VBICloBot22612_0184.

Phylogenomic databases

eggNOGCOG0495.
HOGENOMHOG000200748.
KOK01869.
OMAGIEHACM.
OrthoDBEOG63Z74X.
ProtClustDBPRK00390.

Enzyme and pathway databases

BioCycCBOT413999:GJ72-231-MONOMER.
CBOT441771:GIWX-217-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_00049_B. Leu_tRNA_synth_B.
InterProIPR002300. aa-tRNA-synth_Ia.
IPR002302. Leu-tRNA-ligase_bac/mito.
IPR025709. Leu_tRNA-synth_edit.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PANTHERPTHR11946:SF7. PTHR11946:SF7. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF13603. tRNA-synt_1_2. 1 hit.
[Graphical view]
PRINTSPR00985. TRNASYNTHLEU.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00396. leuS_bact. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYL_CLOBH
AccessionPrimary (citable) accession number: A5HY79
Secondary accession number(s): A7G094
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries