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Q5B1Z0 (CCPR2_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Putative heme-binding peroxidase

EC=1.11.1.-
Gene names
ORF Names:AN5440
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeEmericella

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity.

Sequence similarities

Belongs to the peroxidase family. Cytochrome c peroxidase subfamily.

Ontologies

Keywords
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processresponse to oxidative stress

Inferred from electronic annotation. Source: InterPro

   Molecular functionheme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Putative heme-binding peroxidase
PRO_0000055587

Sites

Active site381Proton acceptor By similarity
Active site1781Tryptophan radical intermediate By similarity
Metal binding1621Iron (heme axial ligand) By similarity
Site341Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5B1Z0 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: FEF3CFBF0E54C880

FASTA31234,521
        10         20         30         40         50         60 
MSKPGDYNAV RRDIAAQLKK PGYDDGSAGP VFVRLAWHSS GTYDAASDTG GSNGAGMRYE 

        70         80         90        100        110        120 
AEGGDPANAG LQHGRAFLEP VKEKHPWITY SDLWTLAGVV AIEEMGGPKI PWLPGRTDFV 

       130        140        150        160        170        180 
DDSKVPPRGR LPDGAQGADH LRFIFYRMGF NDQEIVALAG GHNLGRCHAD RSGFQGPWVN 

       190        200        210        220        230        240 
NPTRFSNQFF KLLLNMEWKP KTLENGVSQF VYIDPEAEDH EEPLMMLPTD VALRDDPAFR 

       250        260        270        280        290        300 
PWVERYAKDK DLFFDHFSKA FAKLIELGIQ RDASGKVTNT DNVKGGYHSA PKKSDEPTGP 

       310 
PRPHTAQRAA KL 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACD01000094 Genomic DNA. Translation: EAA62600.1.
BN001305 Genomic DNA. Translation: CBF81905.1.
RefSeqXP_663044.1. XM_657952.1.

3D structure databases

ProteinModelPortalQ5B1Z0.
ModBaseSearch...

Protein family/group databases

PeroxiBase3835. AniCcP01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00003649; CADANIAP00003649; CADANIAG00003649.
GeneID2871733.
KEGGani:AN5440.2.

Phylogenomic databases

OMANNPTRFS.
OrthoDBEOG45HW63.
PhylomeDBQ5B1Z0.

Family and domain databases

InterProIPR002207. Asc_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
KOK00435.
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00459. ASPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS00435. PEROXIDASE_1. False negative.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCCPR2_EMENI
AccessionPrimary (citable) accession number: Q5B1Z0
Secondary accession number(s): C8VGI0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: April 26, 2005
Last modified: January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families