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Q8FMI8 (SYC_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. 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
Synonyms:cysS1
Ordered Locus Names:CE2516
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length459 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.

Sequence caution

The sequence BAC19326.1 differs from that shown. Reason: Erroneous initiation.

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 – 459459Cysteine--tRNA ligase HAMAP MF_00041
PRO_0000159386

Regions

Motif31 – 4111"HIGH" region HAMAP MF_00041
Motif268 – 2725"KMSKS" region HAMAP MF_00041

Sites

Metal binding291Zinc By similarity
Metal binding2121Zinc By similarity
Metal binding2371Zinc By similarity
Metal binding2411Zinc By similarity
Binding site2711ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FMI8 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: 145FA78B3DED589C

FASTA45950,836
        10         20         30         40         50         60 
MTLRIFDTAT RTLREFIPLK PGHASVYLCG ATPQAQPHIG HVRSGVAFDI LRRWLLAKGL 

        70         80         90        100        110        120 
DVAFVRNVTD IDDKILTKAA EHGRPWWEWV STYEREFTWA YNTLGVLPPS VEPRATGHVT 

       130        140        150        160        170        180 
QMVQYMQRLI DNGFAYEVNG SVYFDVTAWV AAEGSDYGSL SGNRVEDMEQ GETDNFGKRG 

       190        200        210        220        230        240 
PQDFALWKAA KPGEPSWPTP WGEGRPGWHL ECSAMATYYL GAEFDIHCGG LDLQFPHHEN 

       250        260        270        280        290        300 
EIAQAHAAGD GFARYWMHNH WVTMAGEKMS KSLGNVLSVP NMLEKVRPVE LRYYLGSAHY 

       310        320        330        340        350        360 
RSVLEYSEGA LTEAAAGYRR IEAFVDRVGE VEVGTWTAGF EAAMDEDLAV PKALAEIHNA 

       370        380        390        400        410        420 
VREGNSALAA GEMEKARELA GAVRAMTGVL GFDPVEWGTQ TDDSAAHEAL EVLVHAELER 

       430        440        450 
RATARAEKDW AVADEVRDRL AAAGIEVVDT ADGVSWKLQ 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC19326.1. Different initiation.
RefSeqNP_739126.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FMI8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1034358.
GenomeReviewsGene locus CE2516 in contig BA000035_GR.
KEGGcef:CE2516.
NMPDRfig|196164.1.peg.2516.
PATRIC21491181. VBICorEff9312_2484.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG327651.
PhylomeDBQ8FMI8.
ProtClustDBPRK00260.

Enzyme and pathway databases

BioCycCEFF196164:CE2516-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_COREF
AccessionPrimary (citable) accession number: Q8FMI8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: January 25, 2012
This is version 59 of the entry and version 2 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