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A1W6E1 (SYC_ACISJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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:
Cysteine--tRNA ligase

EC=6.1.1.16
Alternative name(s):
Cysteinyl-tRNA synthetase
Short name=CysRS
Gene names
Name:cysS
Ordered Locus Names:Ajs_1623
OrganismAcidovorax sp. (strain JS42) [Complete proteome] [HAMAP]
Taxonomic identifier232721 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). HAMAP MF_00041

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00041

Subunit structure

Monomer By similarity. HAMAP MF_00041

Subcellular location

Cytoplasm HAMAP MF_00041.

Sequence similarities

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

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 458458Cysteine--tRNA ligase HAMAP MF_00041
PRO_0000332779

Regions

Motif31 – 4111"HIGH" region HAMAP MF_00041
Motif270 – 2745"KMSKS" region HAMAP MF_00041

Sites

Metal binding291Zinc By similarity
Metal binding2131Zinc By similarity
Metal binding2381Zinc By similarity
Metal binding2421Zinc By similarity
Binding site2731ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1W6E1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: CAFEE1E186EA1706

FASTA45850,126
        10         20         30         40         50         60 
MSLRIYNTLS RALEEFSPLE PGHVRMYVCG MTVYDLCHLG HARSMIAFDV VQRWLRASGL 

        70         80         90        100        110        120 
AVTYVRNITD IDDKIIKRAV ENGETIRSLT DRMIDALHQD ADALGIERPT HEPRATAYVP 

       130        140        150        160        170        180 
QMLDMIGTLQ GKGLAYQAGN GDVNYAVRKF PGYGKLSGKS LDELNAGERV AVQDGKHDPL 

       190        200        210        220        230        240 
DFVLWKSAKP EEPADVKWRS PFGEGRPGWH IECSAMGCAL LGESFDIHGG GADLQFPHHE 

       250        260        270        280        290        300 
NEIAQSEGAT GKPFARLWMH NGFINVDNEK MSKSLGNFFT IRDVLKEYDA ETVRFFVVRS 

       310        320        330        340        350        360 
HYRSPLNYSN VHLDDARAAL KRLYTALSLV APAPVEVDWA EGYAARFKAA MDEDFGTPEA 

       370        380        390        400        410        420 
VAVLFDLAGE VNRSKSPAAA GLLKALGGHL GLLQADPQDF LKAGAGLDEA AIQAQIAARA 

       430        440        450 
TAKAAKNFAE ADRIRNDLLA QGIVLKDSAS GTTWEAAQ 

« Hide

References

[1]"Complete sequence of chromosome 1 of Acidovorax sp. JS42."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000539 Genomic DNA. Translation: ABM41816.1.
RefSeqYP_985892.1. NC_008782.1.

3D structure databases

ProteinModelPortalA1W6E1.
SMRA1W6E1. Positions 3-401.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1W6E1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4674710.
GenomeReviewsGene locus Ajs_1623 in contig CP000539_GR.
KEGGajs:Ajs_1623.
PATRIC20688564. VBIAciSp27161_1821.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0215.
HOGENOMHBG327651.
OMADFDALNM.
PhylomeDBA1W6E1.
ProtClustDBPRK00260.

Enzyme and pathway databases

BioCycASP232721:AJS_1623-MONOMER.

Family and domain databases

HAMAPMF_00041. Cys_tRNA_synth.
[Tree]
InterProIPR015803. Cys-tRNA-synt.
IPR015273. Cys-tRNA-synt_Ia_DALR.
IPR024909. Cys-tRNA/MSH_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01883.
PANTHERPTHR10890. Cys_tRNA-synt_1a. 1 hit.
PfamPF09190. DALR_2. 1 hit.
PF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSPR00983. TRNASYNTHCYS.
SMARTSM00840. DALR_2. 1 hit.
[Graphical view]
SUPFAMSSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR00435. CysS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYC_ACISJ
AccessionPrimary (citable) accession number: A1W6E1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families