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B6YQU1 (SYC_AZOPC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. 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:CFPG_300
OrganismAzobacteroides pseudotrichonymphae genomovar. CFP2 [Complete proteome] [HAMAP]
Taxonomic identifier511995 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesCandidatus Azobacteroides

Protein attributes

Sequence length492 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 By similarity 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 – 492492Cysteine--tRNA ligase 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

Sequences

Sequence LengthMass (Da)Tools
B6YQU1 [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

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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP010656 Genomic DNA. Translation: BAG83563.1.
RefSeqYP_002308974.1. NC_011565.1.

3D structure databases

ProteinModelPortalB6YQU1.
ModBaseSearch...

Protein-protein interaction databases

STRINGB6YQU1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7039294.
GenomeReviewsGene locus CFPG_300 in contig AP010656_GR.
KEGGaps:CFPG_300.
PATRIC31962267. VBICanAzo57536_0509.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG327651.
OMANVFDIHG.
ProtClustDBPRK00260.

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. 2 hits.
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_AZOPC
AccessionPrimary (citable) accession number: B6YQU1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 20, 2009
Last modified: January 25, 2012
This is version 25 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