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Reviewed, UniProtKB/Swiss-Prot Q82GD0 (SYC1_STRAW)

Last modified November 3, 2009. Version 42. 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 1
    EC=6.1.1.16
Alternative name(s):
    Cysteine--tRNA ligase 1
      Short name=CysRS 1
Gene names
Name: cysS1
Ordered Locus Names: SAV_3967
OrganismStreptomyces avermitilis [Complete proteome] [HAMAP]
Taxonomic identifier33903 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Subunit structure

Monomer By similarity.

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 – 466466Cysteinyl-tRNA synthetase 1 HAMAP MF_00041
PRO_0000159488

Regions

Motif31 – 4111"HIGH" region HAMAP MF_00041
Motif264 – 2685"KMSKS" region HAMAP MF_00041

Sites

Metal binding291Zinc By similarity
Metal binding2081Zinc By similarity
Metal binding2331Zinc By similarity
Metal binding2371Zinc By similarity
Binding site2671ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82GD0-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 64B00ECC32961E23

FASTA46652,242
        10         20         30         40         50         60 
MTIRLYDTSA RQIRDFTPLL PGCVSIYLCG ATVQAAPHIG HIRSGLNFDI MRRWFEYRGY 

        70         80         90        100        110        120 
DVTFIRNVTD IDDKIIAKSA DHGRPWWAIG YENERAFNDG YDVLGCLPPT YEPRATGHIT 

       130        140        150        160        170        180 
EMVEMMRTLI ERGHAYEADG NVYFDVRSFP EYLQLSNQEL DNLLQPSGEG ETGKRDPRDF 

       190        200        210        220        230        240 
AMWKAAKPGE PTWETPWGRG RPGWHLECSA MAHKYLGSAF DIHGGGLDLI FPHHENEIAQ 

       250        260        270        280        290        300 
AKAFGDEFAR YWVHNAWVTM SGEKMSKSLG NSVLVSEMVK QWRPIVLRYY LGTPHYRSMI 

       310        320        330        340        350        360 
EYSEEALREA ESAFARIEGF VQRVVEKAGG VVEPSPEVPP AFAEAMDDDL GVPQALAIVH 

       370        380        390        400        410        420 
TTVRQGNSAL AADDKEAAVA RLAEVRAMLG VLGLDPLDPQ WAGEGDRGED LHGVVDTLVR 

       430        440        450        460 
MVLDQREAAR ARKDWATADA IRDQLNQSGL VIEDSPQGPR WTLGPR 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases

BA000030 Genomic DNA. Translation: BAC71679.1.
RefSeqNP_825144.1.

3D structure databases

HSSPHSSP built from PDB template 1LI5 based on UniProtKB P21888.
ModBaseSearch...

Genome annotation databases

GeneID1210850.
GenomeReviewsGene locus SAV_3967 in contig BA000030_GR.
KEGGsma:SAV_3967.
NMPDRfig|227882.1.peg.3970.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ82GD0.
OMAVLWKAAK.

Enzyme and pathway databases

BioCycSAVE227882:SAV3967-MON.
BRENDA6.1.1.16. 140873.

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...

Entry information

Entry nameSYC1_STRAW
AccessionPrimary (citable) accession number: Q82GD0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 42 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