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Q0SE24 (Q0SE24_RHOSR) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names
Gene names
Ordered Locus Names:RHA1_ro02407 EMBL ABG94212.1
OrganismRhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP] EMBL ABG94212.1
Taxonomic identifier101510 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region57 – 582Sulfate 1 binding PDB 3QNS
Region244 – 2463Chloride 3 binding PDB 3VED

Sites

Metal binding2261Iron (heme axial ligand); via tele nitrogen PDB 3QNR PDB 3QNS PDB 3VEC PDB 3VED PDB 3VEE PDB 3VEF PDB 3VEG PDB 4HOV
Binding site1121Sulfate 1 PDB 3QNS
Binding site1131Chloride 1 PDB 3VEE PDB 3VEG PDB 4HOV
Binding site1131Sulfate 2 PDB 3QNS
Binding site1381Chloride 1 PDB 3VEC PDB 3VED PDB 3VEF PDB 4HOV
Binding site1411Sulfate 1 PDB 3QNS
Binding site2441Chloride 2 PDB 3VEC

Sequences

Sequence LengthMass (Da)Tools
Q0SE24 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 92E794073EE0EAC3

FASTA35037,222
        10         20         30         40         50         60 
MPGPVARLAP QAVLTPPSAA SLFLVLVAGD SDDDRATVCD VISGIDGPLK AVGFRELAGS 

        70         80         90        100        110        120 
LSCVVGVGAQ FWDRVSASSK PAHLHPFVPL SGPVHSAPST PGDLLFHIKA ARKDLCFELG 

       130        140        150        160        170        180 
RQIVSALGSA ATVVDEVHGF RYFDSRDLLG FVDGTENPTD DDAADSALIG DEDPDFRGGS 

       190        200        210        220        230        240 
YVIVQKYLHD MSAWNTLSTE EQERVIGRTK LENVELDDDA QPSNSHVTLN TIVDDDGVEH 

       250        260        270        280        290        300 
DILRDNMAFG SLGEAEYGTY FIGYAKDPAV TELMLRRMFL GEPPGNYDRV LDFSTAATGT 

       310        320        330        340        350 
LFFVPSRDVL ESLGDEPAGA ESAPEDPVEP AAAGPYDLSL KIGGLKGVSQ 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse."
McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H. expand/collapse author list , Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W., Eltis L.D.
Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RHA1.
[2]"Characterization of dye-decolorizing peroxidases from Rhodococcus jostii RHA1."
Roberts J.N., Singh R., Grigg J.C., Murphy M.E., Bugg T.D., Eltis L.D.
Biochemistry 50:5108-5119(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH HEME AND SULFATE.
[3]"Distal heme pocket residues of B-type dye-decolorizing peroxidase: arginine but not aspartate is essential for peroxidase activity."
Singh R., Grigg J.C., Armstrong Z., Murphy M.E., Eltis L.D.
J. Biol. Chem. 287:10623-10630(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH CHLORIDE AND HEME.
[4]"Improved manganese-oxidizing activity of DypB, a peroxidase from a lignolytic bacterium."
Singh R., Grigg J.C., Qin W., Kadla J.F., Murphy M.E., Eltis L.D.
ACS Chem. Biol. 8:700-706(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH CHLORIDE AND HEME.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000431 Genomic DNA. Translation: ABG94212.1.
RefSeqYP_702370.1. NC_008268.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QNRX-ray2.25A/B/C1-350[»]
3QNSX-ray1.40A1-350[»]
3VECX-ray2.60A/B/C1-350[»]
3VEDX-ray2.50A/B/C1-350[»]
3VEEX-ray2.40A/B/C1-350[»]
3VEFX-ray2.64A/B/C1-350[»]
3VEGX-ray2.35A/B/C1-350[»]
4HOVX-ray2.20A/B/C1-350[»]
ProteinModelPortalQ0SE24.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING101510.RHA1_ro02407.

Proteomic databases

PRIDEQ0SE24.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG94212; ABG94212; RHA1_ro02407.
GeneID4219959.
KEGGrha:RHA1_ro02407.
PATRIC23203675. VBIRhoJos26306_2437.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2837.
HOGENOMHOG000151980.
KOK07223.
OMATVDFLDD.
OrthoDBEOG6N682X.

Enzyme and pathway databases

BioCycRJOS101510:GJJ1-2405-MONOMER.

Family and domain databases

InterProIPR011008. Dimeric_a/b-barrel.
IPR006314. Dyp_peroxidase.
[Graphical view]
PfamPF04261. Dyp_perox. 1 hit.
[Graphical view]
SUPFAMSSF54909. SSF54909. 1 hit.
TIGRFAMsTIGR01413. Dyp_perox_fam. 1 hit.
PROSITEPS51404. DYP_PEROXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ0SE24.

Entry information

Entry nameQ0SE24_RHOSR
AccessionPrimary (citable) accession number: Q0SE24
Entry history
Integrated into UniProtKB/TrEMBL: September 5, 2006
Last sequence update: September 5, 2006
Last modified: June 11, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)