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A5FYD2 (SYC_ACICJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:Acry_1404
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium

Protein attributes

Sequence length449 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 – 449449Cysteine--tRNA ligase HAMAP MF_00041
PRO_0000332777

Regions

Motif32 – 4211"HIGH" region HAMAP MF_00041
Motif268 – 2725"KMSKS" region HAMAP MF_00041

Sites

Metal binding301Zinc By similarity
Metal binding2101Zinc By similarity
Metal binding2351Zinc By similarity
Metal binding2391Zinc By similarity
Binding site2711ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5FYD2 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: A2DC6B6698FAA6A1

FASTA44948,863
        10         20         30         40         50         60 
MIQIKLHNTK TRRREPFAPA DPAHVKLYVC GPTVYDRAHL GNARTVVVFD TLVRLLRHLF 

        70         80         90        100        110        120 
PRVTYVRNIT DIDDKINARA AETGETIGEI TARTTSWFHE DMAALYCAPP DIEPRATGHI 

       130        140        150        160        170        180 
GDIIALIERL IARGHAYAAE GHVLFAVATD AEYGKFSGRS PEELLAGARV DVATYKRDPG 

       190        200        210        220        230        240 
DFVLWKPSPP DLPGWDSPWG RGRPGWHIEC SAMIHATLGE TIDIHGGGAD LIFPHHENEI 

       250        260        270        280        290        300 
AQSCCAFPGS EFARVWVHAG MLQVDGQKMS KSLGNFRTVQ DVLGEAPGEA VRFLLLKTHY 

       310        320        330        340        350        360 
RGVLDFSTAA LAEAKRELDR FYRALEKHAD PAPAATPPAA FIEALADDLN TPGAIAELHA 

       370        380        390        400        410        420 
LADAAMQGDA ASAAGLRAAG MLIGIFNHTA DQWFRGEATD DARIDALIAE RLAARRNKDF 

       430        440 
ARADAIRAEL AAAGILLEDG PGGTTWRRA 

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000697 Genomic DNA. Translation: ABQ30614.1.
RefSeqYP_001234533.1. NC_009484.1.

3D structure databases

ProteinModelPortalA5FYD2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5FYD2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5160514.
GenomeReviewsGene locus Acry_1404 in contig CP000697_GR.
KEGGacr:Acry_1404.
PATRIC20647826. VBIAciCry6074_1901.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0215.
HOGENOMHBG327651.
OMANVFDIHG.
ProtClustDBPRK00260.

Enzyme and pathway databases

BioCycACRY349163:ACRY_1404-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. 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_ACICJ
AccessionPrimary (citable) accession number: A5FYD2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: June 12, 2007
Last modified: January 25, 2012
This is version 36 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