Uncharacterized protein - Rhodococcus sp. (strain RHA1)

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Q0SE24 (Q0SE24_RHOSR) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 43. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Submitted name:
Uncharacterized protein EMBL ABG94212.1

Gene names

Ordered Locus Names:

RHA1_ro02407 EMBL ABG94212.1

Organism

Rhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP] EMBL ABG94212.1

Taxonomic identifier

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus ›

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Heme PDB 3QNR PDB 3QNS Iron Metal-binding
Technical term	3D-structure PDB 3QNR PDB 3QNS PDB 3VEC PDB 3VED PDB 3VEE PDB 3VEF PDB 3VEG PDB 4HOV Complete proteome
Gene Ontology (GO)
Molecular_function	heme binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW peroxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

1

Iron (heme axial ligand); via tele nitrogen PDB 3QNR PDB 3QNS

Sequences

Sequence

Length

Mass (Da)

Tools

Q0SE24 [UniParc].

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

350

37,222

        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

References

	« Hide 'large scale' referencesShow '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. 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.
[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).
[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. 0:0-0(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000431 Genomic DNA. Translation: ABG94212.1.

RefSeq

YP_702370.1. NC_008268.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QNR	X-ray	2.25	A/B/C	1-350	[»]
3QNS	X-ray	1.40	A	1-350	[»]
3VEC	X-ray	2.60	A/B/C	1-350	[»]
3VED	X-ray	2.50	A/B/C	1-350	[»]
3VEE	X-ray	2.40	A/B/C	1-350	[»]
3VEF	X-ray	2.64	A/B/C	1-350	[»]
3VEG	X-ray	2.35	A/B/C	1-350	[»]
4HOV	X-ray	2.20	A/B/C	1-350	[»]

ProteinModelPortal

ModBase

Protein-protein interaction databases

STRING

101510.RHA1_ro02407.

Protocols and materials databases

StructuralBiologyKnowledgebase

Genome annotation databases

EnsemblBacteria

ABG94212; ABG94212; RHA1_ro02407.

GeneID

KEGG

rha:RHA1_ro02407.

PATRIC

23203675. VBIRhoJos26306_2437.

Organism-specific databases

CMR

Phylogenomic databases

eggNOG

HOGENOM

KO

OMA

ProtClustDB

Enzyme and pathway databases

BioCyc

RJOS101510:GJJ1-2405-MONOMER.

Family and domain databases

InterPro

IPR011008. Dimeric_a/b-barrel.
IPR006314. Dyp_peroxidase.
[Graphical view]

Pfam

PF04261. Dyp_perox. 1 hit.
[Graphical view]

SUPFAM

SSF54909. Dimer_A_B_barrel. 1 hit.

TIGRFAMs

TIGR01413. Dyp_perox_fam. 1 hit.

PROSITE

PS51404. DYP_PEROXIDASE. 1 hit.
[Graphical view]

ProtoNet

Other

EvolutionaryTrace

Entry information

Entry name

Q0SE24_RHOSR

Accession

Primary (citable) accession number: Q0SE24

Entry history

Integrated into UniProtKB/TrEMBL:	September 5, 2006
Last sequence update:	September 5, 2006
Last modified:	May 29, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info