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Protein
Submitted name:

Uncharacterized protein

Gene

RHA1_ro02407

Organism
Rhodococcus jostii (strain RHA1)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi226 – 2261Iron (heme axial ligand); via tele nitrogenCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

HemeCombined sources, Iron, Metal-binding

Enzyme and pathway databases

BioCyciRJOS101510:GJJ1-2405-MONOMER.
BRENDAi1.11.1.14. 10764.
1.11.1.16. 10764.

Names & Taxonomyi

Protein namesi
Submitted name:
Uncharacterized proteinImported
Gene namesi
Ordered Locus Names:RHA1_ro02407Imported
OrganismiRhodococcus jostii (strain RHA1)Imported
Taxonomic identifieri101510 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus
ProteomesiUP000008710 Componenti: Chromosome

PTM / Processingi

Proteomic databases

PRIDEiQ0SE24.

Interactioni

Protein-protein interaction databases

STRINGi101510.RHA1_ro02407.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ0SE24.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0SE24.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2837.
HOGENOMiHOG000151980.
KOiK07223.
OMAiAIFMEAM.
OrthoDBiEOG6N682X.

Family and domain databases

InterProiIPR011008. Dimeric_a/b-barrel.
IPR006314. Dyp_peroxidase.
[Graphical view]
PfamiPF04261. Dyp_perox. 1 hit.
[Graphical view]
SUPFAMiSSF54909. SSF54909. 1 hit.
TIGRFAMsiTIGR01413. Dyp_perox_fam. 1 hit.
PROSITEiPS51404. DYP_PEROXIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0SE24-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGPVARLAP QAVLTPPSAA SLFLVLVAGD SDDDRATVCD VISGIDGPLK
60 70 80 90 100
AVGFRELAGS LSCVVGVGAQ FWDRVSASSK PAHLHPFVPL SGPVHSAPST
110 120 130 140 150
PGDLLFHIKA ARKDLCFELG RQIVSALGSA ATVVDEVHGF RYFDSRDLLG
160 170 180 190 200
FVDGTENPTD DDAADSALIG DEDPDFRGGS YVIVQKYLHD MSAWNTLSTE
210 220 230 240 250
EQERVIGRTK LENVELDDDA QPSNSHVTLN TIVDDDGVEH DILRDNMAFG
260 270 280 290 300
SLGEAEYGTY FIGYAKDPAV TELMLRRMFL GEPPGNYDRV LDFSTAATGT
310 320 330 340 350
LFFVPSRDVL ESLGDEPAGA ESAPEDPVEP AAAGPYDLSL KIGGLKGVSQ
Length:350
Mass (Da):37,222
Last modified:September 5, 2006 - v1
Checksum:i92E794073EE0EAC3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000431 Genomic DNA. Translation: ABG94212.1.
RefSeqiWP_011595144.1. NC_008268.1.
YP_702370.1. NC_008268.1.

Genome annotation databases

EnsemblBacteriaiABG94212; ABG94212; RHA1_ro02407.
GeneIDi4219959.
KEGGirha:RHA1_ro02407.
PATRICi23203675. VBIRhoJos26306_2437.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000431 Genomic DNA. Translation: ABG94212.1.
RefSeqiWP_011595144.1. NC_008268.1.
YP_702370.1. NC_008268.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ0SE24.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi101510.RHA1_ro02407.

Proteomic databases

PRIDEiQ0SE24.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABG94212; ABG94212; RHA1_ro02407.
GeneIDi4219959.
KEGGirha:RHA1_ro02407.
PATRICi23203675. VBIRhoJos26306_2437.

Phylogenomic databases

eggNOGiCOG2837.
HOGENOMiHOG000151980.
KOiK07223.
OMAiAIFMEAM.
OrthoDBiEOG6N682X.

Enzyme and pathway databases

BioCyciRJOS101510:GJJ1-2405-MONOMER.
BRENDAi1.11.1.14. 10764.
1.11.1.16. 10764.

Miscellaneous databases

EvolutionaryTraceiQ0SE24.

Family and domain databases

InterProiIPR011008. Dimeric_a/b-barrel.
IPR006314. Dyp_peroxidase.
[Graphical view]
PfamiPF04261. Dyp_perox. 1 hit.
[Graphical view]
SUPFAMiSSF54909. SSF54909. 1 hit.
TIGRFAMsiTIGR01413. Dyp_perox_fam. 1 hit.
PROSITEiPS51404. DYP_PEROXIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RHA1Imported.
  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.
  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 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 HEME.

Entry informationi

Entry nameiQ0SE24_RHOJR
AccessioniPrimary (citable) accession number: Q0SE24
Entry historyi
Integrated into UniProtKB/TrEMBL: September 5, 2006
Last sequence update: September 5, 2006
Last modified: June 24, 2015
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.