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Reviewed, UniProtKB/Swiss-Prot B6YQU1 (SYC_AZOPC)

Last modified October 13, 2009. Version 9. 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

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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: CFPG_300
OrganismAzobacteroides pseudotrichonymphae genomovar. CFP2 [Complete proteome] [HAMAP]
Taxonomic identifier511995 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Candidatus Azobacteroides

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Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Cysteinyl-tRNA synthetase HAMAP MF_00041
PRO_1000090816

Regions

Motif33 – 4311"HIGH" region HAMAP MF_00041
Motif283 – 2875"KMSKS" region HAMAP MF_00041

Sites

Metal binding311Zinc By similarity
Metal binding2261Zinc By similarity
Metal binding2511Zinc By similarity
Metal binding2551Zinc By similarity
Binding site2861ATP By similarity

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Sequences

Sequence LengthMass (Da)Tools
B6YQU1-1 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: 762FBEDB8DA9B972

FASTA49256,682
        10         20         30         40         50         60 
MKNQLFIYNT LTGRKELFQS LYPKRVGLYV CGPTVYGDPH LGHARPAITF DILFRYLMHL 

        70         80         90        100        110        120 
NYKVRYVRNI TDVGHLTSDS DLGEDKIARK ARLEDLEPME VVQHYLNLYH KTMDALNVLP 

       130        140        150        160        170        180 
PSIEPHASAH IIEQIQLIKE ILEKGYAYES KGSVYFDVEK YNKKYNYGKL SGQNIADMLN 

       190        200        210        220        230        240 
TTRKLDGQEG KRNPIDFALW KKASSKHIMQ WISPWSNGFP GWHLECTTMS RKYLGNLFDI 

       250        260        270        280        290        300 
HGGGMDLIFP HHECEIAQKV ASTGYEGVKY WMHNNMVTVN GQKMGKSSNN FINLEQLFNG 

       310        320        330        340        350        360 
TNPLLIQSYN PMTVRFFILQ SHYRNTIDFS NKALQASKKG LSRLLEANNN IKQLTAQTTN 

       370        380        390        400        410        420 
STVNIEGLRN KSIEAMNDDL NTPIIISYLF EATRIVNSAL AKQTQLTTED IQQLKDFFQL 

       430        440        450        460        470        480 
FLFNLLGIKD ELKYKNTSYN SFAKAVDLLL QIRVQAKQEK NWIFADKIRD ELTVLGFEVK 

       490 
DTKNGFEWKL SK

« Hide

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References

[1]"Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT protist cells in termite gut."
Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.
Science 322:1108-1109(2008) [PubMed: 19008447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

AP010656 Genomic DNA. Translation: BAG83563.1.
RefSeqYP_002308974.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7039294.
GenomeReviewsGene locus CFPG_300 in contig AP010656_GR.
KEGGaps:CFPG_300.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_00041.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR015804. 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.
[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.
TIGRFAMsTIGR00435. cysS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSYC_AZOPC
AccessionPrimary (citable) accession number: B6YQU1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 20, 2009
Last modified: October 13, 2009
This is version 9 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)

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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