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Reviewed, UniProtKB/Swiss-Prot Q5P1H8 (SYC_AZOSE)

Last modified February 9, 2010. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cysteinyl-tRNA synthetase
    EC=6.1.1.16
Alternative name(s):
    Cysteine--tRNA ligase
      Short name=CysRS
Gene names
Name: cysS
Ordered Locus Names: AZOSEA27110
ORF Names: ebA4792
OrganismAzoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

Protein attributes

Sequence length461 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

cysteine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Cysteinyl-tRNA synthetase HAMAP MF_00041
PRO_0000159342

Regions

Motif30 – 4011"HIGH" region HAMAP MF_00041
Motif269 – 2735"KMSKS" region HAMAP MF_00041

Sites

Metal binding281Zinc By similarity
Metal binding2121Zinc By similarity
Metal binding2371Zinc By similarity
Metal binding2411Zinc By similarity
Binding site2721ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5P1H8-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 4BEC8BF9DBEA7612

FASTA46151,978
        10         20         30         40         50         60 
MLHIHNTLTR RKEAFVPIAP GKVRMYVCGM TVYDYCHLGH ARVMVVFDMV ARWLRASGFE 

        70         80         90        100        110        120 
LTYVRNITDI DDKIIRRAGE KGESIRTLTD RFIAAMHEDA DALGVLRPDH EPRATEYVMQ 

       130        140        150        160        170        180 
MQSLIGRLRD KGLAYVAGNR DVCYSVRKFD SYGRFSGKSL DELRAGERVE VAGDKQDPLD 

       190        200        210        220        230        240 
FVLWKHARTD EPDEVKWASP WGAGRPGWHI ECSAMSSDLL GEQFDIHGGG QDLQFPHHEN 

       250        260        270        280        290        300 
EIAQSEGAHG HTFVNYWMHN GFVRVDDEKM SKSLGNFFTI RDVLERFDPE VVRFFILRAH 

       310        320        330        340        350        360 
YRSPLNYSDA HLEDARQALT RLYTALRNVQ PSDAQVDWDE PHAMRFRAAM DDDFNTAEAV 

       370        380        390        400        410        420 
AVLFELANEA NRSGSAATAA QLKGLGGVLG LLAREPASFL QGRMAGEPDK GEGVAIESMI 

       430        440        450        460 
ERRALAKKSK DYAEADRIRA QLLASGIVLE DTPHGTVWRR A 

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR555306 Genomic DNA. Translation: CAI08836.1.
RefSeqYP_159737.1.

3D structure databases

SMRQ5P1H8. Positions 1-400, 23-437.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5P1H8.

Genome annotation databases

GeneID3180031.
GenomeReviewsGene locus AZOSEA27110 in contig CR555306_GR.
KEGGeba:ebA4792.
NMPDRfig|76114.4.peg.2608.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0215.
HOGENOMHBG327651.
OMAVLWKAAK.

Enzyme and pathway databases

BioCycASP76114:EBA4792-MONOMER.

Family and domain databases

HAMAPMF_00041_B. Cys_tRNA_synth_B.
[Tree]
InterProIPR015804. Cys-tRNA-synt_Ia_C.
IPR015273. Cys-tRNA-synt_Ia_DALR.
IPR015803. Cys-tRNA-synt_Ia_N.
IPR002308. Cys-tRNA-synth_1a.
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.
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]
TIGRFAMsTIGR00435. cysS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYC_AZOSE
AccessionPrimary (citable) accession number: Q5P1H8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 4, 2005
Last modified: February 9, 2010
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents